Structure of PDB 1jpm Chain D

Receptor sequence

>1jpmD (length=358) Species: 1423 (Bacillus subtilis)

MKIIRIETSRIAVPLTKPFKTALRTVYTAESVIVRITYDSGAVGWGEAPP
TLVITGDSMDSIESAIHHVLKPALLGKSLAGYEAILHDIQHLLTGNMSAK
AAVEMALYDGWAQMCGLPLYQMLGGYRDTLETDYTVSVNSPEEMAADAEN
YLKQGFQTLKIKVGKDDIATDIARIQEIRKRVGSAVKLRLDANQGWRPKE
AVTAIRKMEDAGLGIELVEQPVHKDDLAGLKKVTDATDTPIMADESVFTP
RQAFEVLQTRSADLINIKLMKAGGISGAEKINAMAEACGVECMVGSMIET
KLGITAAAHFAASKRNITRFDFDAPLMLKTDVFNGGITYSGSTISMPGKP
GLGIIGAA

3D structure

• PDB: 1jpm Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis.
• Chain: D
• Resolution: 2.25 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F19 P50 V53 T135 K160 K162 L190 D191 A192 N193 E219 D244 E245 S246 N266 K268 G295 S296 M297 F320 D321 F322
• Catalytic site (residue number reindexed from 1): F19 P50 V53 T135 K160 K162 L190 D191 A192 N193 E219 D244 E245 S246 N266 K268 G295 S296 M297 F320 D321 F322
• Enzyme Commision number: 5.1.1.20: L-Ala-D/L-Glu epimerase.

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	MG	D	D191 E219 D244	D191 E219 D244

Gene Ontology

Molecular Function

• GO:0016853 isomerase activity
• GO:0016854 racemase and epimerase activity
• GO:0016855 racemase and epimerase activity, acting on amino acids and derivatives
• GO:0046872 metal ion binding
• GO:0103031 L-Ala-D/L-Glu epimerase activity

Biological Process

• GO:0016998 cell wall macromolecule catabolic process
• GO:0071555 cell wall organization

External links

• PDB: RCSB:1jpm, PDBe:1jpm, PDBj:1jpm
• PDBsum: 1jpm
• PubMed: 11747448
• UniProt: O34508|AEEP_BACSU L-Ala-D/L-Glu epimerase (Gene Name=ykfB)