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4Q4I

Crystal structure of E.coli aminopeptidase N in complex with amastatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AHIS297
AHIS301
AGLU320
CL2O1

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 902
ChainResidue
ASER332
AASP333
AGLY335
AHOH1284

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 903
ChainResidue
AASP452
AHOH1176
AHOH1387
AARG161

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 904
ChainResidue
AGLN19
AILE20
ALEU138
AHOH1158
AHOH1224

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 905
ChainResidue
ALEU532
ATRP546
AASP566
AALA567
ASER570
AHOH1125

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 906
ChainResidue
ASER63
AVAL64
ATRP71
ATRP74
AARG669
AVAL670
AGLU671
AGOL907
AHOH1441

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 907
ChainResidue
ATHR72
ATRP74
AVAL670
AGOL906

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 908
ChainResidue
AARG681
AALA707
AASN708
AASN709
AASP712
AHOH1256
AHOH1389

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 909
ChainResidue
AGLU409
AASP412
ASER590
ALEU591
AHOH1475

site_idBC1
Number of Residues21
DetailsBINDING SITE FOR CHAIN C OF AMASTATIN
ChainResidue
AGLN119
AGLU121
AASN259
AMET260
AGLY261
AALA262
AMET263
AGLU264
ALYS274
ATYR275
AHIS297
AGLU298
AHIS301
ALYS319
AGLU320
ATYR376
ATYR381
AARG783
AARG825
AZN901
CHOH101

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW
ChainResidueDetails
AVAL294-TRP303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865
ChainResidueDetails
AGLU298

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AGLU121
AGLY261
AHIS297
AHIS301
AGLU320

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305
ChainResidueDetails
ATYR381

223166

PDB entries from 2024-07-31

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