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2HPT

Crystal Structure of E. coli PepN (Aminopeptidase N)in complex with Bestatin

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
ABES960

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE BES A 960
ChainResidue
AHIS297
AGLU298
AHIS301
ALYS319
AGLU320
AASN373
ATYR376
ATYR381
AZN950
AHOH1611
AHOH1695
AGLU121
AMET260
AGLY261
AALA262
AGLU264

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 971
ChainResidue
ASER63
AVAL64
ATRP71
ATHR72
ATRP74
AARG669
AVAL670
AGLU671
AHOH1092
AHOH1201
AHOH1531

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 972
ChainResidue
ALEU532
ATRP546
AASP566
ASER570

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 973
ChainResidue
ATHR72
ATRP74
AVAL670
AGLU671
AHOH1440
AHOH1531

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
ATYR299

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AALA122
AALA262
AGLU298
AASN302
AGLY321

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305
ChainResidueDetails
AGLU382

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1h19
ChainResidueDetails
AGLU264
AGLU298
ATYR381

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PDB entries from 2024-07-24

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