5LF0
Human 20S proteasome complex with Epoxomicin at 2.4 Angstrom
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064014 | 3000131 | SCOP2B (2022-06-29) |
O | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064014 | 3000131 | SCOP2B (2022-06-29) |
K | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079492 | 3000131 | SCOP2B (2022-06-29) |
Y | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079492 | 3000131 | SCOP2B (2022-06-29) |
BA [auth b] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079175 | 3000131 | SCOP2B (2022-06-29) |
N | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079175 | 3000131 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064036 | 3000131 | SCOP2B (2022-06-29) |
P | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064036 | 3000131 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064004 | 3000131 | SCOP2B (2022-06-29) |
Q | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064004 | 3000131 | SCOP2B (2022-06-29) |
R | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064022 | 3000131 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064022 | 3000131 | SCOP2B (2022-06-29) |
S | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064060 | 3000131 | SCOP2B (2022-06-29) |
E | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064060 | 3000131 | SCOP2B (2022-06-29) |
F | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064054 | 3000131 | SCOP2B (2022-06-29) |
T | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064054 | 3000131 | SCOP2B (2022-06-29) |
V | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064074 | 3000131 | SCOP2B (2022-06-29) |
H | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064074 | 3000131 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Proteasome | e5lf0A1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
O | Proteasome | e5lf0O1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
J | Proteasome | e5lf0J1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
X | Proteasome | e5lf0X1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
K | Proteasome | e5lf0K1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
Y | Proteasome | e5lf0Y1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
L | Proteasome | e5lf0L1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
Z | Proteasome | e5lf0Z1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
AA [auth a] | Proteasome | e5lf0a1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
M | Proteasome | e5lf0M1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
BA [auth b] | Proteasome | e5lf0b1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
N | Proteasome | e5lf0N1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
B | Proteasome | e5lf0B1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
P | Proteasome | e5lf0P1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
C | Proteasome | e5lf0C1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
Q | Proteasome | e5lf0Q1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
R | Proteasome | e5lf0R1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
D | Proteasome | e5lf0D1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
S | Proteasome | e5lf0S1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
E | Proteasome | e5lf0E1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
F | Proteasome | e5lf0F1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
T | Proteasome | e5lf0T1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
G | Proteasome | e5lf0G1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
U | Proteasome | e5lf0U1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
V | Proteasome | e5lf0V1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
H | Proteasome | e5lf0H1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
I | Proteasome | e5lf0I1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
W | Proteasome | e5lf0W1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: Proteasome | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
AA [auth a], M | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain |
BA [auth b], N | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain | |
PF12465 | Proteasome beta subunits C terminal (Pr_beta_C) | Proteasome beta subunits C terminal | - | Family | |
PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Pharos: Disease Associations Pharos Homepage Annotation
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
6V1 | Parent Component: CYS | |
6VO | ||
ACE | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 | :  |
IML | Parent Component: ILE :  AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0336 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 , N-methyl-L-isoleucine MOD:00341 | |
YCM | Parent Component: CYS :  AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0336 | |
6V1 | Parent Component: CYS :  AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0336 | |
6V1 | Parent Component: CYS :  AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0336 | |
YCM | Parent Component: CYS :  AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0336 |