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4Q4E

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

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
ABB2902

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE BB2 A 902
ChainResidue
ATYR275
AHIS297
AGLU298
AHIS301
AGLU320
AASP327
ATYR376
ATYR381
AARG783
AARG825
AZN901
AGOL903
AHOH1780
AHOH1994
AASN259
AMET260
AGLY261
AALA262
AGLU264

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 903
ChainResidue
ATYR275
AASP290
AARG293
ABB2902

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 904
ChainResidue
AASN623
AGLY791
AARG832
AHOH1783
AHOH1911

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 905
ChainResidue
ATHR393
ALEU394
AASN507
AHOH1329
AHOH1593

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 906
ChainResidue
ATHR393
AALA486
AGLU535
AHOH1509

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 907
ChainResidue
ASER112
APHE194
AASP216
AALA254
AVAL255
AASP256
AHOH1478
AHOH1819

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 908
ChainResidue
AGLU627
ALEU628
APHE629
AASP630
AARG835

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 909
ChainResidue
ATRP74
AGLU671
AHOH1135
AHOH1923

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 910
ChainResidue
APHE704
AGLU734
ATYR735
ALYS738
ATRP739
AHOH1835

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 911
ChainResidue
ATHR26
AVAL35
ATHR37

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

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PDB entries from 2024-10-16

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