Structure of PDB 3cb3 Chain C Binding Site BS03

Receptor Information
>3cb3 Chain C (length=357) Species: 296591 (Polaromonas sp. JS666) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SDRITWVRISSCYLPLMTEIAILFAEIETAGGHQGLGFSYSKRAGGPGQF
AHAREIAPALIGEDPSDIAKLWDKLCWAGASAGRSGLSTQAIGAFDVALW
DLKAKRAGLSLAKLLGSYRDSVRCYNTSGGFLHTPIDQLMVNASASIERG
IGGIKLKVGQPDGALDIARVTAVRKHLGDAVPLMVDANQQWDRPTAQRMC
RIFEPFNLVWIEEPLDAYDHEGHAALALQFDTPIATGEMLTSAAEHGDLI
RHRAADYLMPDAPRVGGITPFLKIASLAEHAGLMLAPHFAMELHVHLAAA
YPREPWVEHFEWLEPLFNERIEIRDGRMLVPTRPGLGLTLSGQVKAWTRE
EAQVGTR
Ligand information
Ligand IDLGT
InChIInChI=1S/C6H10O8/c7-1(3(9)5(11)12)2(8)4(10)6(13)14/h1-4,7-10H,(H,11,12)(H,13,14)/t1-,2-,3-,4+/m1/s1
InChIKeyDSLZVSRJTYRBFB-AJSXGEPRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(C(C(=O)O)O)O)(C(C(=O)O)O)O
ACDLabs 10.04O=C(O)C(O)C(O)C(O)C(O)C(=O)O
CACTVS 3.341O[C@H]([C@@H](O)[C@@H](O)C(O)=O)[C@H](O)C(O)=O
CACTVS 3.341O[CH]([CH](O)[CH](O)C(O)=O)[CH](O)C(O)=O
OpenEye OEToolkits 1.5.0[C@@H]([C@H]([C@H](C(=O)O)O)O)([C@@H](C(=O)O)O)O
FormulaC6 H10 O8
NameL-GLUCARIC ACID
ChEMBL
DrugBank
ZINCZINC000013533920
PDB chain3cb3 Chain C Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3cb3 Crystal structure of L-Talarate dehydratase from Polaromonas sp. JS666 complexed with Mg and L-glucarate.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		K67 K180 K182 D211 E237 E263 H313
Binding residue
(residue number reindexed from 1)		K42 K155 K157 D186 E212 E238 H288
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) S66 T152 K180 K182 D211 N213 E237 G262 E263 M284 D286 H313 F314 A315 E333
Catalytic site (residue number reindexed from 1) S41 T127 K155 K157 D186 N188 E212 G237 E238 M259 D261 H288 F289 A290 E308
Enzyme Commision number 4.2.1.-
4.2.1.42: galactarate dehydratase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008867 galactarate dehydratase activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:1990594 L-altrarate dehydratase activity
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3cb3, PDBe:3cb3, PDBj:3cb3
PDBsum3cb3
PubMed
UniProtQ12GE3

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