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4IU6

Human Methionine Aminopeptidase in complex with FZ1: Pyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004239molecular_functioninitiator methionyl aminopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006417biological_processregulation of translation
A0006508biological_processproteolysis
A0008235molecular_functionmetalloexopeptidase activity
A0018206biological_processpeptidyl-methionine modification
A0022626cellular_componentcytosolic ribosome
A0031365biological_processN-terminal protein amino acid modification
A0046872molecular_functionmetal ion binding
A0051604biological_processprotein maturation
A0070006molecular_functionmetalloaminopeptidase activity
A0070527biological_processplatelet aggregation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO A 401
ChainResidue
AASP240
AHIS303
ATHR334
AGLU336
AGLU367
ACO402
AHOH552

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 402
ChainResidue
AGLU367
ACO401
AHOH522
AHOH552
AASP229
AASP240

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 403
ChainResidue
AHIS212
AFZ1405
AHOH527
AHOH551
AHOH601

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 404
ChainResidue
ASER205
AASN207
AVAL209
ASER363
AHOH514

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE FZ1 A 405
ChainResidue
ALYS132
ATYR195
ACYS203
AHIS212
ACYS301
AHIS310
ATRP353
ACO403
AHOH527
AHOH551
AHOH768

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
ALYS95
ALEU96
AARG97
AHIS99
AARG218
AGLN221
AHOH558

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 407
ChainResidue
AGLN286
AHOH511
AHOH553
AHOH714
AHOH716

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 Residues53
DetailsZN_FING: C6H2-type => ECO:0000255|PROSITE-ProRule:PRU01357
ChainResidueDetails
ATHR15-LYS68

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03174
ChainResidueDetails
ACYS18
ACYS23
ACYS31
ACYS34
ACYS45
ACYS49
AHIS57
AHIS61

site_idSWS_FT_FI3
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_FI4
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

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AALA11

222415

PDB entries from 2024-07-10

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