Structure of PDB 2hp5 Chain A Binding Site BS01

Receptor Information
>2hp5 Chain A (length=246) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGSITENTSWNKEFSAEAVNGVFVLCKSSSKSCATNDLARASKEYLPAST
FKIPNAIIGLETGVIKNEHQVFKWDGKPRAMKQWERDLTLRGAIQVSAVP
VFQQIAREVGEVRMQKYLKKFSYGNQNISGGIDKFGLEGQLRISAVNQVE
FLESLYLNKLSASKENQLIVKEALVTEAAPEYLVHSKTGFSGVGTESNPG
VAWWVGWVEKETEVYFFAFNMDIDNESKLPLRKSIPTKIMESEGII
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain2hp5 Chain A Residue 269 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2hp5 Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		H203 E227
Binding residue
(residue number reindexed from 1)		H185 E209
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S67 K70 S115 F120 G154 F208
Catalytic site (residue number reindexed from 1) S49 K52 S97 F102 G136 F190
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008658 penicillin binding
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2hp5, PDBe:2hp5, PDBj:2hp5
PDBsum2hp5
PubMed19860471
UniProtP14489|BLO10_PSEAI Beta-lactamase OXA-10 (Gene Name=bla)

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