Structure of PDB 2rjg Chain C

Receptor sequence
>2rjgC (length=353) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLPDA
DAFGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVHNE
EQLAALEEASLDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQ
PVNIVSHFARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQ
SHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLIAVREHKAGEP
VGYGGTWVSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVPIVGRVA
MDMICVDLGPQAQDKAGDPVILWGEGLPVERIKVSAYELITRLTSRVAMK
YVD
3D structure
PDB2rjg 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
ChainC
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 PLP C K34 Y38 L78 H159 A193 S194 R209 G211 I212 Y343 K32 Y36 L76 H157 A191 S192 R207 G209 I210 Y337
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2rjg, PDBe:2rjg, PDBj:2rjg
PDBsum2rjg
PubMed18434499
UniProtP0A6B4|ALR1_ECOLI Alanine racemase, biosynthetic (Gene Name=alr)

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