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4KZA

Crystal structure of AmpC beta-lactamase in complex with fragment 48 (3-(cyclopropylsulfamoyl)thiophene-2-carboxylic acid)

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 Residues8
DetailsBINDING SITE FOR RESIDUE NZ9 A 401
ChainResidue
ALEU254
ASER257
APRO306
AHOH686
BGLN250
BGLN253
BLEU254
BSER257

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NZ9 A 402
ChainResidue
APRO26
AILE48
ATYR203
ALYS342
AHOH689
AHOH830
ALYS24

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NZ9 A 403
ChainResidue
AGLN261
ATHR262
AGLY263
APRO297
AVAL298
AHOH733
AHOH758
BLYS50
BLYS51

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NZ9 A 404
ChainResidue
ASER64
AGLN120
AASN152
ALEU293
AGLY317
AALA318
ATHR319
ANZ9405
AHOH675
AHOH688

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NZ9 A 405
ChainResidue
AGLN120
AVAL211
ASER212
AGLY320
ANZ9404
AHOH552
AHOH586
AHOH698
AHOH725
AHOH880

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 406
ChainResidue
AHIS13
APHE41
ATHR42
AHOH655
AHOH731
BGLY116
BHOH558

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NZ9 B 401
ChainResidue
BSER64
BLEU119
BGLN120
BASN152
BTYR221
BLEU293
BGLY317
BALA318
BTHR319
BNZ9403
BHOH669
BHOH670

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NZ9 B 402
ChainResidue
AGLN250
AHOH874
BPRO240
BLEU241
BGLN253
BGLN256
BPRO306
BALA307
BARG309
BPRO330
BHOH681

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NZ9 B 403
ChainResidue
BVAL211
BSER212
BTHR319
BGLY320
BNZ9401
BHOH689
BHOH699
BHOH792
BHOH812

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

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PDB entries from 2024-08-07

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