Structure of PDB 3bls Chain B Binding Site BS01

Receptor Information
>3bls Chain B (length=357) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNAL
Ligand information
Ligand IDAPB
InChIInChI=1S/C6H8BNO2/c8-6-3-1-2-5(4-6)7(9)10/h1-4,9-10H,8H2
InChIKeyJMZFEHDNIAQMNB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1cccc(c1)B(O)O
OpenEye OEToolkits 1.5.0B(c1cccc(c1)N)(O)O
ACDLabs 10.04OB(O)c1cccc(N)c1
FormulaC6 H8 B N O2
NameM-AMINOPHENYLBORONIC ACID
ChEMBLCHEMBL20852
DrugBankDB01896
ZINCZINC000169743006
PDB chain3bls Chain B Residue 362 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3bls Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		S64 Y150 T316 G317 A318 N346
Binding residue
(residue number reindexed from 1)		S61 Y147 T313 G314 A315 N343
Annotation score1
Binding affinityBindingDB: Ki=7300nM
Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 Y147 G153 E269 K312 A315
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3bls, PDBe:3bls, PDBj:3bls
PDBsum3bls
PubMed9819201
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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