Structure of PDB 3cb3 Chain C

Receptor sequence

>3cb3C (length=357) Species: 296591 (Polaromonas sp. JS666)

SDRITWVRISSCYLPLMTEIAILFAEIETAGGHQGLGFSYSKRAGGPGQF
AHAREIAPALIGEDPSDIAKLWDKLCWAGASAGRSGLSTQAIGAFDVALW
DLKAKRAGLSLAKLLGSYRDSVRCYNTSGGFLHTPIDQLMVNASASIERG
IGGIKLKVGQPDGALDIARVTAVRKHLGDAVPLMVDANQQWDRPTAQRMC
RIFEPFNLVWIEEPLDAYDHEGHAALALQFDTPIATGEMLTSAAEHGDLI
RHRAADYLMPDAPRVGGITPFLKIASLAEHAGLMLAPHFAMELHVHLAAA
YPREPWVEHFEWLEPLFNERIEIRDGRMLVPTRPGLGLTLSGQVKAWTRE
EAQVGTR

3D structure

• PDB: 3cb3 Crystal structure of L-Talarate dehydratase from Polaromonas sp. JS666 complexed with Mg and L-glucarate.
• Chain: C
• Resolution: 2.0 Å

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.

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	C	D211 E237 E263	D186 E212 E238
BS02	MG	C	A252 F255	A227 F230
BS03	LGT	C	K67 K180 K182 D211 E237 E263 H313	K42 K155 K157 D186 E212 E238 H288

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

External links

• PDB: RCSB:3cb3, PDBe:3cb3, PDBj:3cb3
• PDBsum: 3cb3
• UniProt: Q12GE3