Structure of PDB 3op2 Chain B

Receptor sequence

>3op2B (length=368) Species: 518 (Bordetella bronchiseptica)

SLKITEVKAHALSTPIPERMRVKLNRQMILVEVRTDEGVTGVGSPSGPYD
LAVLKRAIEDVIGPQLIGEDPANINYLWHKVFHGEVSRSVGIAAMSGVDI
ALWDLKGRAMNQPIYQLLGGKFHTRGVRAYASSIYWDLTPDQAADELAGW
VEQGFTAAKLKVGRAPRKDAANLRAMRQRVGADVEILVDANQSLGRHDAL
AMLRILDEAGCYWFEEPLSIDDIEGHRILRAQGTPVRIATGENLYTRNAF
NDYIRNDAIDVLQADASRAGGITEALAISASAASAHLAWNPHTFNDIITV
AANLHLVAASPHPAMFEWDITHNDLMTRLASYDLKLENGLVQPPQGPGLG
FEIDWDFVAAHAWKGEPA

3D structure

• PDB: 3op2 Crystal structure of putative mandelate racemase from Bordetella bronchiseptica RB50 complexed with 2-oxoglutarate/phosphate
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M21 G54 D57 S144 K171 K173 D201 N203 E227 G253 E254 N255 Q275 D277 H304 T305 F306 E329 I332 H334
• Catalytic site (residue number reindexed from 1): M20 G47 D50 S132 K159 K161 D189 N191 E215 G241 E242 N243 Q263 D265 H292 T293 F294 E317 I320 H322

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	D201 E227 E254	D189 E215 E242

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0016836 hydro-lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009063 amino acid catabolic process
• GO:0016052 carbohydrate catabolic process

External links

• PDB: RCSB:3op2, PDBe:3op2, PDBj:3op2
• PDBsum: 3op2
• UniProt: A0A0H3LT39