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3B3B

Crystal structure of E. coli Aminopeptidase N in complex with tryptophan

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 950
ChainResidue
AHIS297
AHIS301
AGLU320
ATRP900

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 951
ChainResidue
AHOH1502
ASER332
AASP333
AGLY335
AHOH1119
AHOH1265

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 952
ChainResidue
AASP452
AHOH1506

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE TRP A 900
ChainResidue
AGLN119
AGLU121
AMET260
AALA262
AMET263
AGLU264
AHIS297
AGLU298
AHIS301
ALYS319
AGLU320
AASN373
ATYR376
ATYR381
AGLN821
AHOH1111

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLI A 990
ChainResidue
AGLY261
ATYR275
AARG783
AARG825
AHOH1657
AHOH1820
AHOH1834

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 970
ChainResidue
ALEU532
ATRP546
ASER563
AASP566
AALA567
ASER570
AHOH1771
AHOH1793

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 971
ChainResidue
ASER63
ATRP71
ATRP74
AARG669
AGLU671
AHOH1091
AHOH1709

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 972
ChainResidue
AARG681
AGLN703
AALA707
AASN708
AASN709
AASP712
AHOH1289
AHOH1297

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
AHIS301
AGLU320
AGLU121
AGLY261
AHIS297

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

219869

PDB entries from 2024-05-15

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