Structure of PDB 2sfp Chain A

Receptor sequence
>2sfpA (length=379) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
DFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVAR
TALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIA
LTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVALI
ERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHCA
NSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRLV
HVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDGQ
KAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETI
NYEVPCTISYRVPRIFFRHKRIMEVRNAI
3D structure
PDB2sfp Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase.
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) K39 R136 H166 R219 Y265 C311 D313
Catalytic site (residue number reindexed from 1) K37 R134 H164 R217 Y263 C309 D311
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 K39 Y43 H166 S204 R219 G221 I222 Y354 K37 Y41 H164 S202 R217 G219 I220 Y352
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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Cellular Component
External links
PDB RCSB:2sfp, PDBe:2sfp, PDBj:2sfp
PDBsum2sfp
PubMed10079072
UniProtP10724|ALR_GEOSE Alanine racemase (Gene Name=alr)

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