Structure of PDB 1onh Chain A

Receptor sequence
>1onhA (length=363) Species: 550 (Enterobacter cloacae) [Search protein sequence]
PVSEKQLAEVVANTVTPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAAN
KPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDPVTRYWPQLTGKQW
QGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYA
NASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAW
GYRDGKAVRAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASL
KQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPV
AEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPA
RVEAAYHILEALQ
3D structure
PDB1onh Inhibition of Class A and Class C Beta-Lactamases by Penems: Crystallographic Structures of a Novel 1,4-Thiazepine Intermediate
ChainA
Resolution1.38 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) 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 WY4 A S64 L119 Q120 N152 G320 S321 T322 G323 S63 L118 Q119 N151 G319 S320 T321 G322 PDBbind-CN: -logKd/Ki=8.21,IC50=6.2nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1onh, PDBe:1onh, PDBj:1onh
PDBsum1onh
PubMed14609325
UniProtQ59401

[Back to BioLiP]