Annotations: 4FUK

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Creatinase/aminopeptidase catalytic domain-like	8099490	3000126	SCOP2B (2022-06-29)
B	SCOP2 Family	Creatinase/aminopeptidase-like	8099489	4000207	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Creatinase/aminopeptidase catalytic domain-like	8099490	3000126	SCOP2 (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	Peptidase_M24	e4fukA1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Peptidase_M24	ECOD (1.6)
B	Peptidase_M24	e4fukB2	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Peptidase_M24	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)
B	3.90.230.10	Alpha Beta	Alpha-Beta Complex	Creatine Amidinohydrolase	Creatinase/methionine aminopeptidase superfamily	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00557	Metallopeptidase family M24 (Peptidase_M24)	Metallopeptidase family M24	This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Methionine aminopeptidase	peptidase activity catalytic activity, acting on a protein initiator methionyl aminopeptidase activity aminopeptidase activity hydrolase activity exopeptidase activity catalytic activity metallopeptidase activity metalloaminopeptidase activity metalloexopeptidase activity cation binding ion binding binding metal ion binding peptidase activity catalytic activity, acting on a protein initiator methionyl aminopeptidase activity aminopeptidase activity hydrolase activity exopeptidase activity catalytic activity metallopeptidase activity metalloaminopeptidase activity metalloexopeptidase activity cation binding ion binding binding metal ion binding small molecule binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle nucleolus intracellular organelle lumen intracellular organelle organelle lumen organelle intracellular non-membrane-bounded organelle nuclear lumen non-membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR031615	MYND-like zinc finger	Domain
A, B	IPR001714	Peptidase M24, methionine aminopeptidase	Family
A, B	IPR002467	Peptidase M24A, methionine aminopeptidase, subfamily 1	Family
A, B	IPR036005	Creatinase/aminopeptidase-like	Homologous Superfamily
A, B	IPR000994	Peptidase M24	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.