Structure of PDB 4wr3 Chain A

Receptor sequence
>4wr3A (length=359) Species: 562 (Escherichia coli) [Search protein sequence]
MQAATVVINRRALRHNLQRLRELAPASKMVAVVKANAYGHGLLETARTLP
DADAFGVARLEEALRLRAGGITKPVLLLEGFFDARDLPTISAQHFHTAVH
NEEQLAALEEASLDEPVTVWMKLDTGMHRLGVRPEQAEAFYHRLTQCKNV
RQPVNIVSHFARADEPKCGATEKQLAIFNTFCEGKPGQRSIAASGGILLW
PQSHFDWVRPGIILYGVSPLEDRSTGADFGCQPVMSLTSSLIAVREHKAG
EPVGYGGTWVSERDTRLGVVAMGFGDGYPRAAPSGTPVLVNGREVPIVGR
VAMDMICVDLGPQAQDKAGDPVILWGEGLPVERIAEMTKVSAYELITRLT
SRVAMKYVD
3D structure
PDB4wr3 Mechanistic and Evolutionary Insights from the Reciprocal Promiscuity of Two Pyridoxal Phosphate-dependent Enzymes.
ChainA
Resolution1.9 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) 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 K34 Y38 H159 A193 S194 R209 G211 I212 Y343 K34 Y38 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4wr3, PDBe:4wr3, PDBj:4wr3
PDBsum4wr3
PubMed27474741
UniProtP0A6B4|ALR1_ECOLI Alanine racemase, biosynthetic (Gene Name=alr)

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