2B3L

Crystal structure of type I human methionine aminopeptidase in the apo form

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	6
Details	BINDING SITE FOR RESIDUE K A 403

Chain	Residue
A	SER205
A	ASN207
A	VAL209
A	SER363
A	HOH665
A	HOH768

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 470

Chain	Residue
A	VAL206
A	VAL209
A	ILE214
A	ASP216
A	ARG218
A	HOH511
A	HOH547
A	THR172
A	THR204
A	SER205

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site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 471

Chain	Residue
A	HIS212
A	CYS301
A	HIS310
A	GLU336
A	HOH543
A	HOH634
A	HOH683
A	HOH821
A	HOH825
A	HOH978

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACY A 472

Chain	Residue
A	PHE198
A	CYS203
A	HOH634
A	HOH882

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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

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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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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
A	ASN314
A	GLU336

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1a16

Chain	Residue	Details
A	GLU336

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