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4XN2

Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-Leucine

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
ALEU902

site_idAC2
Number of Residues13
Detailsbinding site for residue LEU A 902
ChainResidue
AGLU298
AHIS301
ALYS319
AGLU320
ATYR376
ATYR381
AZN901
AHOH1441
AGLN119
AGLU121
AALA262
AGLU264
AHIS297

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 903
ChainResidue
ASER332
AASP333
AGLY335
AHOH1594
AHOH1680
AHOH1843

site_idAC4
Number of Residues6
Detailsbinding site for residue NA A 904
ChainResidue
AASP452
AGOL915
AHOH1614
AHOH1729
AHOH1809
AHOH1816

site_idAC5
Number of Residues5
Detailsbinding site for residue NA A 905
ChainResidue
AGLU426
AASP432
ASER434
AHOH1491
AHOH1822

site_idAC6
Number of Residues5
Detailsbinding site for residue NA A 906
ChainResidue
ASER48
ALEU86
AHOH1045
AHOH1588
AHOH1664

site_idAC7
Number of Residues5
Detailsbinding site for residue NA A 907
ChainResidue
ATHR347
AHOH1359
AHOH1679
AHOH1832
AHOH1845

site_idAC8
Number of Residues6
Detailsbinding site for residue NA A 908
ChainResidue
AGLU371
AHOH1009
AHOH1083
AHOH1123
AHOH1252
AHOH1813

site_idAC9
Number of Residues5
Detailsbinding site for residue NA A 909
ChainResidue
AGLN19
AILE20
ALEU138
AHOH1580
AHOH1819

site_idAD1
Number of Residues5
Detailsbinding site for residue NA A 910
ChainResidue
ATYR185
AGLU264
AGLY305
AASN306
ALYS319

site_idAD2
Number of Residues6
Detailsbinding site for residue NA A 911
ChainResidue
AGLY350
AASN623
AGLU627
AHOH1341
AHOH1659
AHOH1744

site_idAD3
Number of Residues6
Detailsbinding site for residue NA A 912
ChainResidue
AARG293
AASN344
AHOH1096
AHOH1100
AHOH1456
AHOH1832

site_idAD4
Number of Residues5
Detailsbinding site for residue NA A 913
ChainResidue
AHIS771
APHE774
AHOH1144
AHOH1524
AHOH1759

site_idAD5
Number of Residues8
Detailsbinding site for residue GOL A 914
ChainResidue
AARG641
ATHR645
AARG686
APHE690
AALA722
AHOH1129
AHOH1297
AHOH1394

site_idAD6
Number of Residues12
Detailsbinding site for residue GOL A 915
ChainResidue
AASP452
ATYR544
ALYS545
AGLN550
ANA904
AHOH1059
AHOH1165
AHOH1266
AHOH1437
AHOH1614
AHOH1729
AHOH1761

site_idAD7
Number of Residues8
Detailsbinding site for residue GOL A 916
ChainResidue
ALYS274
ATYR275
AARG783
AARG825
AHOH1292
AHOH1866
AALA260
AGLY261

site_idAD8
Number of Residues4
Detailsbinding site for residue MLI A 917
ChainResidue
AARG728
AASP729
AMET732
AGLN753

site_idAD9
Number of Residues4
Detailsbinding site for residue MLI A 918
ChainResidue
AGLN587
APRO588
ALEU589
AALA643

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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