Structure of PDB 4rdy Chain A

Receptor sequence
>4rdyA (length=313) Species: 985053 (Vulcanisaeta moutnovskia 768-28) [Search protein sequence]
VRISIAGGNEIDPGSMGLTLFHEHLRLITEVVRWNWPHLYNEDEELKRAI
DAVNAAKKYGVKTIIDLTVAGIGCDVRFNEKVAKATGVNIIMGTGFYTYT
EIPFYFKNRGIDSLVDAFVHDITIGIQGTNTRAAFVKAVIDSSGLTKDVE
MAIRAAAKAHIKTDVPIITHSFVGNKSSLDLIRIFKEEGVDLARTVIGHV
GDTDDISFIEQILREGAFIGLDRFGLDIYLPLDKRVKTAIELIKRGWIDQ
LLLSHDYCPTIDWYPPEVVRSTVPDWTMTLIFEKVIPRMRSEGITEEQIN
RVLIDNPRRLFTG
3D structure
PDB4rdy Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia.
ChainA
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) H22 H24 K137 H170 H199 D202 R223 D256
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 A H23 H25 K138 D257 H22 H24 K137 D256
BS02 CO A K138 H171 H200 K137 H170 H199
BS03 3M5 A H25 L28 Y98 K138 H171 R224 L227 D257 C259 W264 Y265 H24 L27 Y97 K137 H170 R223 L226 D256 C258 W263 Y264
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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