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3B2P

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

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 950
ChainResidue
AHIS297
AHIS301
AGLU320
AARG900

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 951
ChainResidue
AHOH1281
ASER332
AASP333
AGLY335
AHOH1050
AHOH1132

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 952
ChainResidue
AASP452
AHOH1203
AHOH1553
AHOH1717

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ARG A 900
ChainResidue
AGLN119
AGLU121
AALA262
AGLU264
AHIS297
AGLU298
AHIS301
ALYS319
AGLU320
AASN373
ATYR376
ATYR381
AGLN821
AHOH1362
AHOH1377
AHOH1681

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLI A 990
ChainResidue
AARG641
AGLU642
ATHR645
AARG686
AALA722
AHOH1232
AHOH1408
AHOH1658

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 970
ChainResidue
ALEU532
ATRP546
AASP566
AALA567
ASER570
AHOH1388

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 971
ChainResidue
AMET260
ATYR376
ATHR377
ALEU378
ATYR381
AGLU382
AHOH1612

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 972
ChainResidue
AMET260
AGLY261
ALYS274
ATYR275
AARG293
AARG783
AARG825
AHOH1753

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 973
ChainResidue
ASER63
ATRP71
ATRP74
AARG669
AGLU671
AHOH1129

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 974
ChainResidue
ALEU61
ATRP74
AARG669
AGLU671
AHOH1485

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 975
ChainResidue
AGLU409
AASP412
ALEU589
ASER590
ALEU591
AHOH1431
AHOH1449
AHOH1667

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 976
ChainResidue
AGLU69
APRO70
ATRP71
ATHR72
AALA73
AASP221
APRO224
AALA278
ATYR288
AHOH1101
AHOH1423

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 978
ChainResidue
AHIS11
AGLN467
AARG468
ATHR469
AGLN479
APRO480
AALA515
AHOH1532

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 980
ChainResidue
AALA707
AASN708
AASN709
AASP712
AHOH1379
AHOH1404
AARG681
AGLN703

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 981
ChainResidue
APRO473
AASP474
AALA476
AHOH1286
AHOH1707
AHOH1708

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 982
ChainResidue
ATHR72
ATRP74
AGLU671
AHOH1441

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16885166","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18416562","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19622865","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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

239803

PDB entries from 2025-08-06

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