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3B37

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016285molecular_functionalanyl aminopeptidase activity
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 950
ChainResidue
AHIS297
AHIS301
AGLU320
ATYR900
AHOH1688

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 951
ChainResidue
AASP356
AALA361
AHIS362
ATHR379

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 952
ChainResidue
AASP452
AHOH1295
AHOH1730
AHOH1731

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TYR A 900
ChainResidue
AGLN119
AGLU121
AMET260
AALA262
AMET263
AGLU264
AHIS297
AGLU298
AHIS301
AGLU320
AHOH1664
AHOH1687
AHOH1688

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLI A 980
ChainResidue
AARG641
AGLU642
ATHR645
AARG686
AALA722
AHOH1188
AHOH1251
AHOH1665

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 970
ChainResidue
ASER63
ATRP71
ATRP74
AARG669
AGLU671
AHOH1108
AHOH1696

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 971
ChainResidue
ALEU532
ATRP546
AASP566
AALA567
ASER570
AHOH1600

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 972
ChainResidue
AARG681
AGLN703
AALA707
AASN708
AASN709
AASP712
AHOH1247
AHOH1249

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 973
ChainResidue
ALYS8
AGLU123
AASP312
ATRP313
APHE314
AHOH1275
AHOH1459
AHOH1680

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

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 2025-07-02

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