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4XMT

Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-2,3-Diaminopropionic 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 901
ChainResidue
AHIS297
AHIS301
AGLU320
ADPP902

site_idAC2
Number of Residues14
Detailsbinding site for residue DPP A 902
ChainResidue
AGLU298
AHIS301
AGLU320
ATYR381
AZN901
AGOL918
AHOH1010
AHOH1175
AHOH1197
AGLU121
AALA262
AMET263
AGLU264
AHIS297

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 903
ChainResidue
ASER332
AASP333
AGLY335
AHOH1588
AHOH1776
AHOH1877

site_idAC4
Number of Residues6
Detailsbinding site for residue NA A 904
ChainResidue
AASP452
ANA907
AHOH1639
AHOH1885
AHOH1893
AHOH1897

site_idAC5
Number of Residues6
Detailsbinding site for residue NA A 905
ChainResidue
AGLY56
AGLY79
AHOH1393
AHOH1491
AHOH1653
AHOH1718

site_idAC6
Number of Residues5
Detailsbinding site for residue NA A 906
ChainResidue
AGLN19
AILE20
ALEU138
AHOH1728
AHOH1965

site_idAC7
Number of Residues7
Detailsbinding site for residue NA A 907
ChainResidue
AASP452
ATYR544
ANA904
AHOH1179
AHOH1844
AHOH1872
AHOH1897

site_idAC8
Number of Residues6
Detailsbinding site for residue NA A 908
ChainResidue
AHIS771
APHE774
AHOH1191
AHOH1646
AHOH1808
AHOH1865

site_idAC9
Number of Residues4
Detailsbinding site for residue NA A 909
ChainResidue
AASP24
AHOH1112
AHOH1279
AHOH2006

site_idAD1
Number of Residues10
Detailsbinding site for residue GOL A 910
ChainResidue
AHIS11
AARG14
AARG468
ATHR469
ALYS478
AGLN479
APRO480
AHOH1049
AHOH1097
AHOH1498

site_idAD2
Number of Residues7
Detailsbinding site for residue GOL A 911
ChainResidue
AARG641
ATHR645
AARG686
AALA722
AHOH1124
AHOH1208
AHOH1445

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL A 912
ChainResidue
ALEU532
ATRP546
AASP566
AALA567
ASER570

site_idAD4
Number of Residues9
Detailsbinding site for residue GOL A 913
ChainResidue
ASER63
AVAL64
ATRP71
ATRP74
AARG669
AVAL670
AGLU671
AHOH1385
AHOH1517

site_idAD5
Number of Residues4
Detailsbinding site for residue GOL A 914
ChainResidue
AGLU292
AVAL670
AHIS672
AHOH1664

site_idAD6
Number of Residues8
Detailsbinding site for residue GOL A 915
ChainResidue
AHOH1192
AHOH1618
AARG681
AGLN703
AALA707
AASN708
AASN709
AASP712

site_idAD7
Number of Residues6
Detailsbinding site for residue GOL A 916
ChainResidue
AGLU409
AASP412
ASER590
ALEU591
AHOH1215
AHOH1476

site_idAD8
Number of Residues4
Detailsbinding site for residue GOL A 917
ChainResidue
AASP281
ALYS738
ATRP739
AHOH1130

site_idAD9
Number of Residues10
Detailsbinding site for residue GOL A 918
ChainResidue
AGLN119
AGLU121
AALA260
AASN373
ATYR376
AGLN821
ADPP902
AHOH1175
AHOH1356
AHOH1741

site_idAE1
Number of Residues7
Detailsbinding site for residue MLI A 919
ChainResidue
AALA260
AGLY261
ALYS274
ATYR275
AARG783
AARG825
AHOH1156

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

219869

PDB entries from 2024-05-15

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