Structure of PDB 1blc Chain A

Receptor sequence
>1blcA (length=257) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
KELNDLEKKYNAHIGVYALDTKSGKEVKFNSDKRFAYASTSKAINSAILL
EQVPYNKLNKKVHINKDDIVAYSPILEKYVGKDITLKALIEASMTYSDNT
ANNKIIKEIGGIKKVKQRLKELGDKVTNPVRYEIELNYYSPKSKKDTSTP
AAFGKTLNKLIANGKLSKENKKFLLDLMLNNKSGDTLIKDGVPKDYKVAD
KSGQAITYASRNDVAFVYPKGQSEPIVLVIFTNKDNKSDKPNDKLISETA
KSVMKEF
3D structure
PDB1blc Inhibition of beta-lactamase by clavulanate. Trapped intermediates in cryocrystallographic studies.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 Q237
Catalytic site (residue number reindexed from 1) S39 K42 S97 E133 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 CEM A A69 S70 S130 K234 S235 G236 Q237 A38 S39 S97 K201 S202 G203 Q204
BS02 TEM A S70 Y105 N132 G236 Q237 I239 S39 Y72 N99 G203 Q204 I206
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:1blc, PDBe:1blc, PDBj:1blc
PDBsum1blc
PubMed1569569
UniProtP00807|BLAC_STAAU Beta-lactamase (Gene Name=blaZ)

[Back to BioLiP]