5OHM

K33-specific affimer bound to K33 diUb

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ubiquitin-like	8098438	3000157	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	Ubiquitin-like	8098438	3000157	SCOP2B (2022-06-29)
C [auth E]	SCOP2 Family	Ubiquitin-related	8098437	4000962	SCOP2 (2022-06-29)
C [auth E]	SCOP2 Superfamily	Ubiquitin-like	8098438	3000157	SCOP2 (2022-06-29)
D [auth G]	SCOP2B Superfamily	Ubiquitin-like	8098438	3000157	SCOP2B (2022-06-29)
E [auth I]	SCOP2B Superfamily	Ubiquitin-like	8098438	3000157	SCOP2B (2022-06-29)
F [auth K]	SCOP2B Superfamily	Ubiquitin-like	8098438	3000157	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)
H	Cystatin	e5ohmH1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
I [auth L]	Cystatin	e5ohmL1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
J [auth B]	Cystatin	e5ohmB1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
K [auth F]	Cystatin	e5ohmF1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
L [auth J]	Cystatin	e5ohmJ1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
G [auth D]	Cystatin	e5ohmD1	A: a+b two layers	X: Cystatin-like	H: Cystatin/monellin (From Topology)	T: Cystatin/monellin	F: Cystatin	ECOD (1.6)
A	ubiquitin_1	e5ohmA1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ubiquitin_1	ECOD (1.6)
B [auth C]	ubiquitin_1	e5ohmC1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ubiquitin_1	ECOD (1.6)
C [auth E]	ubiquitin_1	e5ohmE1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ubiquitin_1	ECOD (1.6)
D [auth G]	ubiquitin_1	e5ohmG1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ubiquitin_1	ECOD (1.6)
E [auth I]	ubiquitin_1	e5ohmI1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ubiquitin_1	ECOD (1.6)
F [auth K]	ubiquitin_1	e5ohmK1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ubiquitin_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	PF00240	Ubiquitin family (ubiquitin)	Ubiquitin family	This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry ...	This family contains a number of ubiquitin-like proteins: SUMO (smt3 homologue) (see Swiss:Q02724), Nedd8 (see Swiss:P29595), Elongin B (see Swiss:Q15370), Rub1 (see Swiss:Q9SHE7), and Parkin (see Swiss:O60260). A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites [5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
G [auth D], H, I [auth L], J [auth B], K [auth F], G [auth D], H, I [auth L], J [auth B], K [auth F], L [auth J]	K33-specific affimer	-	-	-
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	Polyubiquitin-C	protein tag activity molecular tag activity ubiquitin protein ligase binding protein binding binding ubiquitin-like protein ligase binding enzyme binding	catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process protein ubiquitination macromolecule modification post-translational protein modification catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process protein ubiquitination macromolecule modification post-translational protein modification protein modification process protein modification by small protein conjugation protein modification by small protein conjugation or removal	membrane-bounded organelle intracellular anatomical structure mitochondrial membrane mitochondrion membrane organelle outer membrane cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle organelle envelope bounding membrane of organelle organelle mitochondrial envelope mitochondrial outer membrane membrane-bounded organelle intracellular anatomical structure mitochondrial membrane mitochondrion membrane organelle outer membrane cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle organelle envelope bounding membrane of organelle organelle mitochondrial envelope mitochondrial outer membrane outer membrane cytoplasm organelle membrane nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	IPR019956	Ubiquitin domain	Domain
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	IPR019954	Ubiquitin conserved site	Conserved Site
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	IPR050158	Ubiquitin and ubiquitin-like	Family
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	IPR029071	Ubiquitin-like domain superfamily	Homologous Superfamily
A, B [auth C], C [auth E], D [auth G], E [auth I], A, B [auth C], C [auth E], D [auth G], E [auth I], F [auth K]	IPR000626	Ubiquitin-like domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.