Structure of PDB 1epv Chain A

Receptor sequence

>1epvA (length=382) Species: 1422 (Geobacillus stearothermophilus)

NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVA
RTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRI
ALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVAL
IERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHC
ANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRL
VHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDG
QKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLET
INYEVPCTISYRVPRIFFRHKRIMEVRNAIGR

3D structure

• PDB: 1epv A side reaction of alanine racemase: transamination of cycloserine.
• Chain: A
• Resolution: 2.2 Å

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	DCS	A	K39 Y43 L85 R136 H166 S204 R219 G221 I222 Y354	K38 Y42 L84 R135 H165 S203 R218 G220 I221 Y353
BS02	DCS	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

External links

• PDB: RCSB:1epv, PDBe:1epv, PDBj:1epv
• PDBsum: 1epv
• PubMed: 12741835
• UniProt: P10724|ALR_GEOSE Alanine racemase (Gene Name=alr)