Structure of PDB 3ozm Chain G

Receptor sequence

>3ozmG (length=386) Species: 518 (Bordetella bronchiseptica)

SLKITEVKAHALSTPIPERMRVESGAGLKLNRQMILVEVRTDEGVTGVGS
PSGPYDLAVLKRAIEDVIGPQLIGEDPANINYLWHKVFHGEVSRNLGHRS
VGIAAMSGVDIALWDLKGRAMNQPIYQLLGGKFHTRGVRAYASSIYWDLT
PDQAADELAGWVEQGFTAAKLKVGRAPRKDAANLRAMRQRVGADVEILVD
ANQSLGRHDALAMLRILDEAGCYWFEEPLSIDDIEGHRILRAQGTPVRIA
TGENLYTRNAFNDYIRNDAIDVLQADASRAGGITEALAISASAASAHLAW
NPHTFNDIITVAANLHLVAASPHPAMFEWDITHNDLMTRLASYDLKLENG
LVQPPQGPGLGFEIDWDFVAAHAWKGEPAIGAGHGM

3D structure

• PDB: 3ozm Crystal structure of enolase superfamily member from Bordetella bronchiseptica complexed with Mg, m-Xylarate and L-Lyxarate
• Chain: G
• Resolution: 1.6 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 G53 D56 S143 K170 K172 D200 N202 E226 G252 E253 N254 Q274 D276 H303 T304 F305 E328 I331 H333

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	G	D201 E227 E254	D200 E226 E253
BS02	DXL	G	S25 K30 Y147 K171 K173 D201 N203 E254 H304 F306 E329	S24 K29 Y146 K170 K172 D200 N202 E253 H303 F305 E328

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:3ozm, PDBe:3ozm, PDBj:3ozm
• PDBsum: 3ozm
• UniProt: A0A0H3LT39