Structure of PDB 4de0 Chain A Binding Site BS01

Receptor Information
>4de0 Chain A (length=263) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVM
AAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAA
ALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPG
DPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGL
PTSWTAGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRD
VLASAARIIAEGL
Ligand information
Ligand ID0JB
InChIInChI=1S/C15H11N7O/c23-15(11-5-2-6-12-13(11)17-8-16-12)18-10-4-1-3-9(7-10)14-19-21-22-20-14/h1-8H,(H,16,17)(H,18,23)(H,19,20,21,22)
InChIKeyOUXPKPPPOPWHCW-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(c2cccc1ncnc12)Nc3cccc(c3)c4nnnn4
OpenEye OEToolkits 1.7.6c1cc(cc(c1)NC(=O)c2cccc3c2[nH]cn3)c4[nH]nnn4
CACTVS 3.370O=C(Nc1cccc(c1)c2[nH]nnn2)c3cccc4nc[nH]c34
FormulaC15 H11 N7 O
NameN-[3-(1H-tetrazol-5-yl)phenyl]-1H-benzimidazole-7-carboxamide
ChEMBLCHEMBL2031556
DrugBank
ZINCZINC000084670976
PDB chain4de0 Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4de0 Structure-Based Design of Potent and Ligand-Efficient Inhibitors of CTX-M Class A Beta-Lactamase
Resolution1.12 Å
Binding residue
(original residue number in PDB)		N104 Y105 S130 N132 N170 T235 G236 S237 G238 D240
Binding residue
(residue number reindexed from 1)		N79 Y80 S105 N107 N145 T210 G211 S212 G213 D214
Annotation score1
Binding affinityMOAD: Ki=1.3uM
PDBbind-CN: -logKd/Ki=5.89,Ki=1.3uM
Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 S237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 S212
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:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4de0, PDBe:4de0, PDBj:4de0
PDBsum4de0
PubMed22296601
UniProtQ9L5C8

[Back to BioLiP]