Structure of PDB 4rdy Chain B

Receptor sequence
>4rdyB (length=314) Species: 985053 (Vulcanisaeta moutnovskia 768-28) [Search protein sequence]
MVRISIAGGNEIDPGSMGLTLFHEHLRLITEVVRWNWPHLYNEDEELKRA
IDAVNAAKKYGVKTIIDLTVAGIGCDVRFNEKVAKATGVNIIMGTGFYTY
TEIPFYFKNRGIDSLVDAFVHDITIGIQGTNTRAAFVKAVIDSSGLTKDV
EMAIRAAAKAHIKTDVPIITHSFVGNKSSLDLIRIFKEEGVDLARTVIGH
VGDTDDISFIEQILREGAFIGLDRFGLDIYLPLDKRVKTAIELIKRGWID
QLLLSHDYCPTIDWYPPEVVRSTVPDWTMTLIFEKVIPRMRSEGITEEQI
NRVLIDNPRRLFTG
3D structure
PDB4rdy Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H23 H25 K138 H171 H200 D203 R224 D257
Catalytic site (residue number reindexed from 1) H23 H25 K138 H171 H200 D203 R224 D257
Enzyme Commision number ?
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 CO B H23 H25 K138 D257 H23 H25 K138 D257
BS02 CO B K138 H171 H200 K138 H171 H200
BS03 3M5 B H25 L28 Y98 K138 H171 R224 Y230 D257 I262 W264 Y265 T273 H25 L28 Y98 K138 H171 R224 Y230 D257 I262 W264 Y265 T273
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4rdy, PDBe:4rdy, PDBj:4rdy
PDBsum4rdy
PubMed25670483
UniProtF0QXN6

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