Structure of PDB 3i2g Chain A

Receptor sequence
>3i2gA (length=574) Species: 104109 (Rhodococcus sp. MB1 'Bresler 1999') [Search protein sequence]
VDGNYSVASNVMVPMRDGVRLAVDLYRPDADGPVPVLLVRNPYDKFDVFA
WSTQSTNWLEFVRDGYAVVIQDTRGLFASEGEFVPHVDDEADAEDTLSWI
LEQAWCDGNVGMFGVSYLGVTQWQAAVSGVGGLKAIAPSMASADLYRAPW
YGPGGALSVEALLGWSALIGTQLITSRSDARPEDAADFVQLAAILNDVAG
AASVTPLAEQPLLGRLIPWVIDQVVDHPDNDESWQSISLFERLGGLATPA
LITAGWYDGFVGESLRTFVAVKDNADARLVVGPWSHSNLTGRNADRKFGI
AATYPIQEATTMHKAFFDRHLRGETDALAGVPKVRLFVMGIDEWRDETDW
PLPDTAYTPFYLGGSGAANTSTGGGTLSTSISGTESADTYLYDPADPVPS
LGGTLLFHNGDNGPADQRPIHDRDDVLCYSTEVLTDPVEVTGTVSARLFV
SSSAVDTDFTAKLVDVFPDGRAIALCDGIVRMRYRETLVNPTLIEAGEIY
EVAIDMLATSNVFLPGHRIMVQVSSSNFPKYDRNSNTGGVIAREQLEEMC
TAVNRIHRGPEHPSHIVLPIIKRK
3D structure
PDB3i2g Structural analysis of thermostabilizing mutations of cocaine esterase.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y44 S117 Y118 W166 D259 H287
Catalytic site (residue number reindexed from 1) Y43 S116 Y117 W165 D258 H286
Enzyme Commision number 3.1.1.84: cocaine esterase.
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 DBC A Y44 S117 Y118 W151 W166 F261 H287 Y43 S116 Y117 W150 W165 F260 H286
Gene Ontology
Molecular Function
GO:0008239 dipeptidyl-peptidase activity
GO:0016787 hydrolase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0050784 cocaine catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3i2g, PDBe:3i2g, PDBj:3i2g
PDBsum3i2g
PubMed20436035
UniProtQ9L9D7|COCE_RHOSM Cocaine esterase (Gene Name=cocE)

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