Structure of PDB 2sfp Chain B

Receptor sequence

>2sfpB (length=379) Species: 1422 (Geobacillus stearothermophilus)

DFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVAR
TALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIA
LTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVALI
ERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHCA
NSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRLV
HVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDGQ
KAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETI
NYEVPCTISYRVPRIFFRHKRIMEVRNAI

3D structure

• PDB: 2sfp Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase.
• Chain: B
• Resolution: 1.9 Å

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	B	K39 Y43 R136 H166 S204 R219 G221 I222 Y354	K37 Y41 R134 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

External links

• PDB: RCSB:2sfp, PDBe:2sfp, PDBj:2sfp
• PDBsum: 2sfp
• PubMed: 10079072
• UniProt: P10724|ALR_GEOSE Alanine racemase (Gene Name=alr)