Structure of PDB 2rjg Chain A

Receptor sequence

>2rjgA (length=359) Species: 83333 (Escherichia coli K-12)

MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLP
DADAFGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVH
NEEQLAALEEASLDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNV
RQPVNIVSHFARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW
PQSHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLIAVREHKAG
EPVGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVPIVGR
VAMDMICVDLGPQAQDKAGDPVILWGEGLPVERIAEMTKVSAYELITRLT
SRVAMKYVD

3D structure

• PDB: 2rjg Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K34 R129 H159 R209 Y255 A302 D304
• Catalytic site (residue number reindexed from 1): K34 R129 H159 R209 Y255 A302 D304
• Enzyme Commision number: 5.1.1.1: alanine 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	PLP	A	V32 K34 Y38 L78 H159 A193 S194 R209 G211 I212 Y343	V32 K34 Y38 L78 H159 A193 S194 R209 G211 I212 Y343

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008784 alanine racemase activity
• GO:0016853 isomerase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0042803 protein homodimerization activity

Biological Process

• GO:0006522 alanine metabolic process
• GO:0008360 regulation of cell shape
• GO:0009252 peptidoglycan biosynthetic process
• GO:0030632 D-alanine biosynthetic process
• GO:0071555 cell wall organization

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:2rjg, PDBe:2rjg, PDBj:2rjg
• PDBsum: 2rjg
• PubMed: 18434499
• UniProt: P0A6B4|ALR1_ECOLI Alanine racemase, biosynthetic (Gene Name=alr)