Structure of PDB 2mnr Chain A

Receptor sequence

>2mnrA (length=357) Species: 303 (Pseudomonas putida)

EVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATSAGVVGHSYLF
AYTPVALKSLKQLLDDMAAMIVNEPLAPVSLEAMLAKRFCLAGYTGLIRM
AAAGIDMAAWDALGKVHETPLVKLLGANARPVQAYDSHSLDGVKLATERA
VTAAELGFRAVKTKIGYPALDQDLAVVRSIRQAVGDDFGIMVDYNQSLDV
PAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLNVPVQMGENWLGP
EEMFKALSIGACRLAMPDAMKIGGVTGWIRASALAQQFGIPMSSHLFQEI
SAHLLAATPTAHWLERLDLAGSVIEPTLTFEGGNAVIPDLPGVGIIWREK
EIGKYLV

3D structure

• PDB: 2mnr Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V22 S139 K164 K166 D195 N197 E221 G246 E247 D270 M294 H297 L298 F299 A313 E317
• Catalytic site (residue number reindexed from 1): V20 S137 K162 K164 D193 N195 E219 G244 E245 D268 M292 H295 L296 F297 A311 E315
• Enzyme Commision number: 5.1.2.2: mandelate racemase.

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	MN	A	D195 E221 E247	D193 E219 E245

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0016836 hydro-lyase activity
• GO:0016853 isomerase activity
• GO:0018838 mandelate racemase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009063 amino acid catabolic process
• GO:0016052 carbohydrate catabolic process
• GO:0018924 mandelate metabolic process
• GO:0019596 mandelate catabolic process

External links

• PDB: RCSB:2mnr, PDBe:2mnr, PDBj:2mnr
• PDBsum: 2mnr
• PubMed: 1892834
• UniProt: P11444|MANR_PSEPU Mandelate racemase (Gene Name=mdlA)