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4E3L

Crystal structure of AmpC beta-lactamase in complex with a 3-chloro-4-tetrazolyl benzene sulfonamide boronic acid inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 0NB A 401
ChainResidue
ASER64
AHOH788
ATYR150
AASN152
AVAL211
ASER212
AALA318
AGLY320
AHOH785
AHOH787

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
APHE41
ATHR42
AHOH577
AHOH601
AHOH759
AHOH813
BGLY116

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 403
ChainResidue
ATHR262
AGLY263
APRO297
AHOH606
BTYR45
BLYS51

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 404
ChainResidue
ATRP93
ALEU157
ALYS164
AHOH616
AHOH682
AHOH768
AHOH797

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 405
ChainResidue
APRO140
AALA141
ATRP142
AALA143
AHOH771

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 0NB B 401
ChainResidue
ALEU85
AGLN250
ALEU254
ASER257
ATYR259
APRO304
AHOH534
BGLN250
BGLN253
BLEU254
BSER257
BPRO303
BPRO304
BPRO306
BHOH628
BHOH641
BHOH758

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0NB B 402
ChainResidue
BSER64
BGLN120
BTYR150
BASN152
BVAL211
BSER212
BGLY317
BALA318
BGLY320
BHOH739
BHOH741
BHOH747
BHOH755
BHOH774

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 403
ChainResidue
AARG133
AHIS186
AHOH711
AHOH743
AHOH748
BLYS290

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 404
ChainResidue
BARG80
BHOH567

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9
ChainResidueDetails
AGLN120
BGLN120

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY
ChainResidueDetails
AASN152
AALA318
BASN152
BALA318

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM
ChainResidueDetails
AASN343
BASN343

224004

PDB entries from 2024-08-21

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