Structure of PDB 4v2i Chain B

Receptor sequence
>4v2iB (length=315) Species: 1485225 (Thalassospira sp. GB04J01) [Search protein sequence]
PVLEPTTQKFINALSASGGPAIYTLTPAEARDVLSGAQSGEIAKPAVDIT
DTTFAVGPTGATKVRIIRPQGNTDRLPVIVYFHGAGWVMGDTGTHDRLVR
ELSVRANAALVFVDYERSPEARYPVAIEQDYAVTKYVAEHSEQLNVDPTR
LAIAGDSVGGNMTAVVSLLAQERGGPDITAQVLFYPVTDADFDNGSYTEF
ANGPWLTKPAMDWFWNQYLPEGIDRTDPKITPIHATSEQLSGQAPALVIT
AENDVLRDEGEAYARKLSQAGVDVTVTRYNGTIHDFVMLNVLADTPAAKG
AIAQAGQYLHTALHG
3D structure
PDB4v2i Biochemical Characterization and Structural Analysis of a New Cold-Active and Salt-Tolerant Esterase from the Marine Bacterium Thalassospira Sp.
ChainB
Resolution1.686 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A86 G87 S158 V188 F193 D255 H285
Catalytic site (residue number reindexed from 1) A85 G86 S157 V187 F192 D254 H284
Enzyme Commision number 3.1.1.1: carboxylesterase.
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 MG B Y186 T251 D255 R258 Y185 T250 D254 R257
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0106435 carboxylesterase activity

View graph for
Molecular Function
External links
PDB RCSB:4v2i, PDBe:4v2i, PDBj:4v2i
PDBsum4v2i
PubMed27016194
UniProtA0A023T3X2

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