Structure of PDB 1l6g Chain A

Receptor sequence
>1l6gA (length=382) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVA
RTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRI
ALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVAL
IERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHC
ANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRL
VHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDG
QKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLET
INYEVPCTISYRVPRIFFRHKRIMEVRNAIGR
3D structure
PDB1l6g Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K39 R136 H166 R219 Y265 C311 D313
Catalytic site (residue number reindexed from 1) K38 R135 H165 R218 Y264 C310 D312
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 PDD A K39 Y43 R136 H166 S204 R219 G221 I222 Y354 K38 Y42 R135 H165 S203 R218 G220 I221 Y353
BS02 PDD A Y265 C311 M312 Y264 C310 M311
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008784 alanine racemase activity
GO:0016853 isomerase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006522 alanine metabolic process
GO:0009252 peptidoglycan biosynthetic process
GO:0030632 D-alanine biosynthetic process
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:1l6g, PDBe:1l6g, PDBj:1l6g
PDBsum1l6g
PubMed11886871
UniProtP10724|ALR_GEOSE Alanine racemase (Gene Name=alr)

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