1KQ0

Human methionine aminopeptidase type II in complex with D-methionine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0004177	molecular_function	aminopeptidase activity
A	0004239	molecular_function	initiator methionyl aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0016485	biological_process	protein processing
A	0016787	molecular_function	hydrolase activity
A	0018206	biological_process	peptidyl-methionine modification
A	0031365	biological_process	N-terminal protein amino acid modification
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 479

Chain	Residue
A	ASP251
A	ASP262
A	GLU459
A	ZN480
A	MED601

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 480

Chain	Residue
A	ZN479
A	MED601
A	ASP262
A	HIS331
A	GLU364
A	GLU459

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MED A 601

Chain	Residue
A	HIS231
A	ASP251
A	ASP262
A	HIS331
A	HIS339
A	HIS382
A	ZN479
A	ZN480
A	HOH747

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE TBU A 501

Chain	Residue
A	LYS281
A	ASP477

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Functional Information from PROSITE/UniProt

site_id	PS01202
Number of Residues	17
Details	MAP_2 Methionine aminopeptidase subfamily 2 signature. DIcKIDfGtHISGriiD

Chain	Residue	Details
A	ASP246-ASP262

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:16540317

Chain	Residue	Details
A	HIS231
A	HIS339

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946

Chain	Residue	Details
A	ASP251
A	ASP262
A	HIS331
A	GLU364
A	GLU459

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	ALA2

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER45
A	SER74

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER60

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER63

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site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000250

Chain	Residue	Details
A	SER60
A	SER63

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