Structure of PDB 4xbj Chain D

Receptor sequence
>4xbjD (length=351) Species: 562 (Escherichia coli) [Search protein sequence]
ATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLPADA
FGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVHNEEQ
LAALEEASDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNVRQPVN
IVSHFARADEPCGATEKQLAIFNTFCEGKPGQRSIAASGGILLWPQSHFD
WVRPGIILYGVSPLRSTGADFGCQPVMSLTSSLIAVREHKAGEPVGYGGT
WVSERDTRLGVVAMGFGDGYPRAAPSGTPVLVNGREVPIVGRVAMDMICV
DLGPQAQDKAGDPVILWGEGLPVERIAEMTKVSAYELITRLTSRVAMKYV
D
3D structure
PDB4xbj Mechanistic and Evolutionary Insights from the Reciprocal Promiscuity of Two Pyridoxal Phosphate-dependent Enzymes.
ChainD
Resolution2.25 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) K31 R124 H154 R203 Y247 A294 D296
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 IN5 D Y255 A302 M303 Y247 A294 M295
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:4xbj, PDBe:4xbj, PDBj:4xbj
PDBsum4xbj
PubMed27474741
UniProtP0A6B4|ALR1_ECOLI Alanine racemase, biosynthetic (Gene Name=alr)

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