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3B2X

Crystal Structure of E. coli Aminopeptidase N in complex with Lysine

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
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
ALYS960

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 951
ChainResidue
AHOH1721
ASER332
AASP333
AGLY335
AHOH1233
AHOH1364

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 952
ChainResidue
AASP452
AHOH1394
AHOH1625
AHOH1981
AHOH1982

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LYS A 960
ChainResidue
AGLU121
AALA262
AGLU264
AHIS297
AGLU298
AHIS301
AGLU320
AASN373
ATYR376
ATYR381
AHOH1152
AHOH1306
AHOH1323

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MLI A 990
ChainResidue
AARG641
AGLU642
ATHR645
AARG686
APHE690
AHOH1179
AHOH1299
AHOH1686
AHOH1775
AHOH1932
AHOH2044
AHOH2045
AHOH2046

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLI A 991
ChainResidue
AMET260
AGLY261
ATYR275
AARG783
AARG825
AHOH1498
AHOH1918

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLI A 992
ChainResidue
AGLU69
APRO70
ATRP71
ATHR72
APRO224
ATRP225
ATHR280
ATYR288
AHOH1101
AHOH1444

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 970
ChainResidue
ALEU532
ATRP546
AASP566
AALA567
ASER570
AHOH1741

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 971
ChainResidue
ASER63
ATRP71
ATRP74
AARG669
AGLU671
AHOH1087
AHOH1732

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 972
ChainResidue
ALEU61
ATRP74
AARG669
AGLU671
AHOH1600
AHOH1757
AHOH2076
AHOH2083
AHOH2118

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 974
ChainResidue
AARG681
AGLN703
AALA707
AASN708
AASN709
AASP712
AHOH1229
AHOH1292
AHOH1908

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 975
ChainResidue
AMET260
ATYR376
ATHR377
ALEU378
ATYR381
AGLU382
AARG825
AHOH1906
AHOH1918

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 976
ChainResidue
ATYR275
AARG293
AHIS297
ATYR381
AHOH1306
AHOH1342
AHOH1906
AGLY261

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 977
ChainResidue
AASP58
ALEU59
ALYS60
AGLU97
AILE98
AHOH1507
AHOH1886
AHOH2043

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 978
ChainResidue
ATHR393
AALA486
ACYS534
AGLU535
ASER537
AHOH1197
AHOH1395
AHOH2067

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 979
ChainResidue
APHE704
AALA707
ALYS738
ATRP739
AHOH1258
AHOH1673
AHOH2140

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

218853

PDB entries from 2024-04-24

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