4IKU

Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with 2-((5-chloro-6-methyl-2-(pyridin-2-yl)pyrimidin-4-yl)amino)-3-phenylpropanamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SHX A 401

Chain	Residue
A	TYR195
A	HOH567
A	HOH660
A	TYR196
A	CYS203
A	HIS212
A	TYR300
A	HIS310
A	TRP353
A	CO404
A	HOH501

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CO A 402

Chain	Residue
A	ASP240
A	HIS303
A	THR334
A	GLU336
A	GLU367
A	CO403
A	HOH578

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO A 403

Chain	Residue
A	ASP229
A	ASP240
A	GLU367
A	CO402
A	HOH528
A	HOH578

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO A 404

Chain	Residue
A	HIS212
A	SHX401
A	HOH501
A	HOH530
A	HOH549

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 405

Chain	Residue
A	SER205
A	ASN207
A	VAL209
A	SER363
A	HOH513

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Functional Information from PROSITE/UniProt

site_id	PS00680
Number of Residues	19
Details	MAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIHklfHtapnVp.HY

Chain	Residue	Details
A	TYR300-TYR318

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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_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291

Chain	Residue	Details
A	HIS212
A	HIS310

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291

Chain	Residue	Details
A	ASP229
A	ASP240
A	HIS303
A	GLU336
A	GLU367

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