Structure of PDB 1ga0 Chain A

Receptor sequence
>1ga0A (length=363) Species: 550 (Enterobacter cloacae) [Search protein sequence]
PVSEKQLAEVVANTVTPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAAN
KPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDPVTRYWPQLTGKQW
QGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYA
NASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAW
GYRDGKAVRAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASL
KQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPV
AEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPA
RVEAAYHILEALQ
3D structure
PDB1ga0 Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 V121 Y150 G156 E275 K318 S321
Catalytic site (residue number reindexed from 1) S63 K66 Y111 V120 Y149 G155 E274 K317 S320
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 DVR A S64 L119 Q120 Y150 N152 S292 S321 N349 S63 L118 Q119 Y149 N151 S291 S320 N348
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1ga0, PDBe:1ga0, PDBj:1ga0
PDBsum1ga0
PubMed11371184
UniProtQ59401

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