Structure of PDB 2og9 Chain A

Receptor sequence
>2og9A (length=363) Species: 296591 (Polaromonas sp. JS666) [Search protein sequence]
PSDRITWVRISSCYLPLATPIMTEIAILFAEIETAGGHQGLGFSYSKRAG
GPGQFAHAREIAPALIGEDPSDIAKLWDKLCWAGASAGRSGLSTQAIGAF
DVALWDLKAKRAGLSLAKLLGSYRDSVRCYNTSGGFLHTPIDQLMVNASA
SIERGIGGIKLKVGQPDGALDIARVTAVRKHLGDAVPLMVDANQQWDRPT
AQRMCRIFEPFNLVWIEEPLDAYDHEGHAALALQFDTPIATGEMLTSAAE
HGDLIRHRAADYLMPDAPRVGGITPFLKIASLAEHAGLMLAPHFAMELHV
HLAAAYPREPWVEHFEWLEPLFNERIEIRDGRMLVPTRPGLGLTLSGQVK
AWTREEAQVGTRP
3D structure
PDB2og9 Crystal Structure of mandelate racemase/muconate lactonizing enzyme from Polaromonas sp. JS666
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S68 T154 K182 K184 D213 N215 E239 G264 E265 M286 D288 H315 F316 A317 E335
Catalytic site (residue number reindexed from 1) S46 T132 K160 K162 D191 N193 E217 G242 E243 M264 D266 H293 F294 A295 E313
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 CA A A254 F257 A232 F235
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2og9, PDBe:2og9, PDBj:2og9
PDBsum2og9
PubMed
UniProtQ12GE3

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