3C6M
Crystal structure of human spermine synthase in complex with spermine and 5-methylthioadenosine
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | Spermine_synt_N_1 | e3c6mA3 | A: beta meanders | X: Spermidine synthase tetramerisation domain (From Topology) | H: Spermidine synthase tetramerisation domain (From Topology) | T: Spermidine synthase tetramerisation domain | F: Spermine_synt_N_1 | ECOD (1.6) |
A | KOG1562 | e3c6mA1 | A: a+b two layers | X: TBP-like | H: S-adenosylmethionine decarboxylase-related | T: Bacterial S-adenosylmethionine decarboxylase | F: KOG1562 | ECOD (1.6) |
A | Spermine_synth | e3c6mA2 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: Spermine_synth | ECOD (1.6) |
B | Spermine_synt_N_1 | e3c6mB3 | A: beta meanders | X: Spermidine synthase tetramerisation domain (From Topology) | H: Spermidine synthase tetramerisation domain (From Topology) | T: Spermidine synthase tetramerisation domain | F: Spermine_synt_N_1 | ECOD (1.6) |
B | KOG1562 | e3c6mB1 | A: a+b two layers | X: TBP-like | H: S-adenosylmethionine decarboxylase-related | T: Bacterial S-adenosylmethionine decarboxylase | F: KOG1562 | ECOD (1.6) |
B | Spermine_synth | e3c6mB4 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: Spermine_synth | ECOD (1.6) |
C | Spermine_synt_N_1 | e3c6mC2 | A: beta meanders | X: Spermidine synthase tetramerisation domain (From Topology) | H: Spermidine synthase tetramerisation domain (From Topology) | T: Spermidine synthase tetramerisation domain | F: Spermine_synt_N_1 | ECOD (1.6) |
C | Spermine_synth | e3c6mC1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: Spermine_synth | ECOD (1.6) |
D | KOG1562,Spermine_synt_N_1 | e3c6mD1 | A: beta meanders | X: Spermidine synthase tetramerisation domain (From Topology) | H: Spermidine synthase tetramerisation domain (From Topology) | T: Spermidine synthase tetramerisation domain | F: KOG1562,Spermine_synt_N_1 | ECOD (1.6) |
D | Spermine_synth | e3c6mD2 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: Spermine_synth | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF17284 | Spermidine synthase tetramerisation domain (Spermine_synt_N) | Spermidine synthase tetramerisation domain | This domain represents the N-terminal tetramerization domain from spermidine synthase. | Domain | |
PF17950 | S-adenosylmethionine decarboxylase N -terminal (SpmSyn_N) | S-adenosylmethionine decarboxylase N -terminal | This is the N-terminal domain found in human spermine synthase (EC 2.5.1.22). The N-terminal domain, which forms the major part of the dimerization interface, shows a considerable structural similarity to the AdoMetDC-like fold (S-adenosylmethionine ... | Domain | |
PF01564 | Spermine/spermidine synthase domain (Spermine_synth) | Spermine/spermidine synthase domain | Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyses the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase. | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR040900 | Spermine synthase, N-terminal | Domain | |
IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily | Homologous Superfamily | |
IPR037163 | Spermidine synthase, tetramerisation domain superfamily | Homologous Superfamily | |
IPR035246 | Spermidine synthase, tetramerisation domain | Domain | |
IPR015576 | Spermine synthase, animal | Family | |
IPR030374 | Polyamine biosynthesis domain | Domain | |
IPR030373 | Polyamine biosynthesis domain, conserved site | Conserved Site |
Pharos: Disease Associations Pharos Homepage Annotation
Chains | Drug Target   | Associated Disease |
---|---|---|
P52788 | :