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4XMV

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

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
AARG902

site_idAC2
Number of Residues14
Detailsbinding site for residue ARG A 902
ChainResidue
AGLU298
AHIS301
AGLU320
AASN373
ATYR376
ATYR381
AGLN821
AZN901
AHOH1072
AGLU121
AALA260
AALA262
AGLU264
AHIS297

site_idAC3
Number of Residues5
Detailsbinding site for residue NA A 903
ChainResidue
ASER332
AASP333
AGLY335
AHOH1030
AHOH1164

site_idAC4
Number of Residues5
Detailsbinding site for residue NA A 904
ChainResidue
AMET234
ALEU243
AGLU244
ATYR299
AHOH1040

site_idAC5
Number of Residues4
Detailsbinding site for residue NA A 905
ChainResidue
AGLN19
AILE20
ALEU138
AHOH1160

site_idAC6
Number of Residues4
Detailsbinding site for residue GOL A 906
ChainResidue
ALEU532
ATRP546
AASP566
ASER570

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 907
ChainResidue
ALEU61
AVAL62
ASER63
AARG669
AGLU671
AGOL908

site_idAC8
Number of Residues8
Detailsbinding site for residue GOL A 908
ChainResidue
ASER63
AVAL64
APRO70
ATRP71
ATRP74
AARG669
AGLU671
AGOL907

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 909
ChainResidue
AALA260
AGLY261
ALYS274
ATYR275
AARG783
AARG825
AGOL910

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL A 910
ChainResidue
ATYR381
AGLU382
AGOL909
AHOH1011
AHOH1127

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL A 911
ChainResidue
AASN373
ATYR376
AGLN821
AARG825
ALYS864

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL A 912
ChainResidue
ATYR9
AMET368
ATHR472
APRO473
AASP474

site_idAD4
Number of Residues5
Detailsbinding site for residue GOL A 913
ChainResidue
AARG681
AGLN703
AALA707
AASN708
AASP712

site_idAD5
Number of Residues9
Detailsbinding site for residue GOL A 914
ChainResidue
AGLU69
ATRP71
ATHR72
AASP221
AARG222
APRO224
ATRP225
AALA278
ATYR288

site_idAD6
Number of Residues6
Detailsbinding site for residue GOL A 915
ChainResidue
AASP49
AARG53
ASER84
AASP199
ATHR200
ALYS231

site_idAD7
Number of Residues5
Detailsbinding site for residue GOL A 916
ChainResidue
AGLY335
ASER336
AASN340
AHIS672
AILE675

site_idAD8
Number of Residues4
Detailsbinding site for residue MLI A 917
ChainResidue
ALYS738
ATRP739
AASP281
AASN709

site_idAD9
Number of Residues5
Detailsbinding site for residue MLI A 918
ChainResidue
AARG641
ATHR645
AARG686
AALA722
AHOH1006

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

224931

PDB entries from 2024-09-11

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