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2NQ7

Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-Dimethylpropionylamino)pyridine-2-carboxylic acid thiazole-2-ylamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AASP229
AASP240
AGLU367
ACO402
AHOH624
AHOH626

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AGLU336
AGLU367
ACO401
AHOH624
AASP240
AHIS303
ATHR334

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 403
ChainResidue
AHIS212
AHM5410
AHOH476
AHOH547
AHOH625

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 404
ChainResidue
ASER205
AASN207
AVAL209
ASER363
AHOH552

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HM5 A 410
ChainResidue
APRO192
ATYR195
ATYR196
APHE198
ACYS203
AHIS212
AHIS310
ATRP353
ACO403
AHOH476
AHOH625

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 470
ChainResidue
ATHR172
ATHR204
ASER205
AVAL206
AVAL209
AILE214
AASP216
AARG218
AHOH500
AHOH550

Functional Information from PROSITE/UniProt
site_idPS00680
Number of Residues19
DetailsMAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIHklfHtapnVp.HY
ChainResidueDetails
ATYR300-TYR318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AHIS212
AHIS310

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291
ChainResidueDetails
AASP229
AASP240
AHIS303
AGLU336
AGLU367

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AASN314
AGLU336

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a16
ChainResidueDetails
AGLU336

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PDB entries from 2025-06-11

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