1I7M

HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE WITH COVALENTLY BOUND PYRUVOYL GROUP AND COMPLEXED WITH 4-AMIDINOINDAN-1-ONE-2'-AMIDINOHYDRAZONE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Protein Modification Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth B]	d1i7m.1	Alpha and beta proteins (a+b)	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C [auth D]	d1i7m.2	Alpha and beta proteins (a+b)	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B [auth A]	d1i7m.1	Alpha and beta proteins (a+b)	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D [auth C]	d1i7m.2	Alpha and beta proteins (a+b)	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.30.360.50	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
C [auth D]	3.30.360.50	Alpha Beta	2-Layer Sandwich	Dihydrodipicolinate Reductase	domain 2	CATH (4.3.0)
B [auth A]	3.60.90.10	Alpha Beta	4-Layer Sandwich	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	CATH (4.3.0)
D [auth C]	3.60.90.10	Alpha Beta	4-Layer Sandwich	S-adenosylmethionine decarboxylase	S-adenosylmethionine decarboxylase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B [auth A], D [auth C]	PF01536	Adenosylmethionine decarboxylase (SAM_decarbox)	Adenosylmethionine decarboxylase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], C [auth D]	S-ADENOSYLMETHIONINE DECARBOXYLASE BETA CHAIN	cation binding polyamine binding binding ion binding amine binding putrescine binding small molecule binding adenosylmethionine decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity identical protein binding protein binding	polyamine metabolic process amine metabolic process biogenic amine biosynthetic process spermidine metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process metabolic process cellular process spermidine biosynthetic process biogenic amine metabolic process spermine metabolic process spermine biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol
B [auth A], D [auth C]	S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA CHAIN	cation binding polyamine binding binding ion binding amine binding putrescine binding small molecule binding adenosylmethionine decarboxylase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity identical protein binding protein binding	polyamine metabolic process amine metabolic process biogenic amine biosynthetic process spermidine metabolic process biosynthetic process amine biosynthetic process polyamine biosynthetic process metabolic process cellular process spermidine biosynthetic process biogenic amine metabolic process spermine metabolic process spermine biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], C [auth D]	IPR016067	S-adenosylmethionine decarboxylase, core	Homologous Superfamily
A [auth B], C [auth D]	IPR001985	S-adenosylmethionine decarboxylase, eukaryotes	Family
A [auth B], C [auth D]	IPR048283	S-adenosylmethionine decarboxylase-like	Family
A [auth B], C [auth D]	IPR018166	S-adenosylmethionine decarboxylase, conserved site	Conserved Site
B [auth A], D [auth C]	IPR016067	S-adenosylmethionine decarboxylase, core	Homologous Superfamily
B [auth A], D [auth C]	IPR001985	S-adenosylmethionine decarboxylase, eukaryotes	Family
B [auth A], D [auth C]	IPR048283	S-adenosylmethionine decarboxylase-like	Family
B [auth A], D [auth C]	IPR018166	S-adenosylmethionine decarboxylase, conserved site	Conserved Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth B], C [auth D]	Pharos: P17707	glycogen storage disease II ovarian cancer invasive ductal breast carcinoma lung adenocarcinoma
B [auth A], D [auth C]	Pharos: P17707	glycogen storage disease II ovarian cancer invasive ductal breast carcinoma lung adenocarcinoma

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A [auth B], C [auth D]	MSE	Parent Component: MET
B [auth A], D [auth C]	MSE	Parent Component: MET
B [auth A], D [auth C]	PYR	RESID: AA0127 PSI-MOD : pyruvic acid (Cys) MOD:00136 , pyruvic acid (Ser) MOD:00807 , pyruvic acid MOD:01154 , pyruvic acid (Tyr) MOD:01661

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.