Structure of PDB 2rjh Chain D

Receptor sequence

>2rjhD (length=357) Species: 83333 (Escherichia coli K-12)

AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLPDA
DAFGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVHNE
EQLAALEEASLDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQ
PVNIVSHFARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ
SHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLIAVREHKAGEP
VGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVPIVGRVA
MDMICVDLGPQAQDKAGDPVILWGEGLPVERIAEMTKVSAYELITRLTSR
VAMKYVD

3D structure

• PDB: 2rjh 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: D
• 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): K32 R127 H157 R207 Y253 A300 D302
• 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	DCS	D	Y255 A302 M303	Y253 A300 M301
BS02	DCS	D	K34 Y38 R129 H159 A193 S194 R209 G211 I212 Y343	K32 Y36 R127 H157 A191 S192 R207 G209 I210 Y341

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