Structure of PDB 1ghi Chain A

Receptor sequence
>1ghiA (length=257) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
KELNDLEKKYNAHIGVYALDTKSGKEVKFNSDKRFAYASTSKAINSAILL
EQVPYNKLNKKVHINKDDIVAYSPILEKYVGKDITLKALIEASMTYSDNT
ANNKIIKEIGGIKKVKQRLKELGDKVTNPVRYDIELQYYSPKSKKDTSTP
AAFGKTLNKLIANGKLSKENKKFLLDLMLNNKSGDTLIKDGVPKDYKVAD
KSGQAITYASRNDVAFVYPKGQSEPIVLVIFTNKDNKSDKPNDKLISETA
KSVMKEF
3D structure
PDB1ghi Structures of the acyl-enzyme complexes of the Staphylococcus aureus beta-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 D166 K234 Q237
Catalytic site (residue number reindexed from 1) S39 K42 S97 D133 K201 Q204
Enzyme Commision number 3.5.2.6: beta-lactamase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CO3 A S70 S130 S235 S39 S97 S202
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1ghi, PDBe:1ghi, PDBj:1ghi
PDBsum1ghi
PubMed11327855
UniProtP00807|BLAC_STAAU Beta-lactamase (Gene Name=blaZ)

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