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3KED

Crystal structure of Aminopeptidase N in complex with 2,4-diaminobutyric acid

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 875
ChainResidue
AHIS297
AHIS301
AGLU320
ADAB880

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DAB A 880
ChainResidue
AHIS297
AGLU298
AHIS301
ALYS319
AGLU320
ATYR381
AZN875
AMLA991
AGLU121
AMET260
AALA262
AMET263
AGLU264

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 951
ChainResidue
ASER332
AASP333
AGLY335
AHOH949
AHOH1126

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 952
ChainResidue
AASP452
AHOH1210

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 970
ChainResidue
ALEU532
ATRP546
ALEU554
AASP566
ASER570

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 971
ChainResidue
ASER63
AVAL64
ATRP71
ATRP74
AARG669
AVAL670
AGLU671
AGOL972
AGOL975
AHOH980

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 972
ChainResidue
AVAL62
ASER63
ATRP74
AARG669
AGLU671
AGOL971

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 973
ChainResidue
ALEU378
ATYR381
AGLU382
AMLA991

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 974
ChainResidue
AARG681
AALA707
AASN708
AASN709
AASP712
AHOH1290

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 975
ChainResidue
ATHR72
ATRP74
AVAL670
AGLU671
AGOL971
AHOH1222

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 976
ChainResidue
AHIS11
AGLN467
AARG468
ATHR469
AGLN479
APRO480

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 977
ChainResidue
AGLU123
AASP312
ATRP313
APHE314

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 978
ChainResidue
AGLU409
AASP412
ALEU589
ASER590
ALEU591
AHOH1343
AHOH1344

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLA A 990
ChainResidue
AARG641
AGLU642
ATHR645
AARG686
AALA722
AHOH1186
AHOH1283

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MLA A 991
ChainResidue
AARG293
AASP327
ATYR381
ADAB880
AGOL973

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLA A 992
ChainResidue
AGLU69
APRO70
ATRP71
ATHR72
APRO224
AARG279
ATHR280
ATYR288
AHOH994

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

221051

PDB entries from 2024-06-12

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