Structure of PDB 1tkk Chain B

Receptor sequence

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

MKIIRIETSRIAVPLTKPFKTALRTVYTAESVIVRITYDSGAVGWGEAPP
TLVITGDSMDSIESAIHHVLKPALLGKSLAGYEAILHDIQHLLTGNMSAK
AAVEMALYDGWAQMCGLPLYQMLGGYRDTLETDYTVSVNSPEEMAADAEN
YLKQGFQTLKIKVGKDDIATDIARIQEIRKRVGSAVKLRLDANQGWRPKE
AVTAIRKMEDAGLGIELVEQPVHKDDLAGLKKVTDATDTPIMADESVFTP
RQAFEVLQTRSADLINIKLMKAGGISGAEKINAMAEACGVECMVGSMIET
KLGITAAAHFAASKRNITRFDFDAPLMLKTDVFNGGITYSGSTISMPGKP
GLGIIGAA

3D structure

• PDB: 1tkk Evolution of Enzymatic Activities in the Enolase Superfamily: Structure of a Substrate-Liganded Complex of the l-Ala-d/l-Glu Epimerase from Bacillus subtilis(,).
• Chain: B
• Resolution: 2.1 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	B	D191 E219 D244	D191 E219 D244
BS02	ALA	B	K162 D321 D323	K162 D321 D323
BS03	GLU	B	F19 R24 I54 K268 S296 I298	F19 R24 I54 K268 S296 I298

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:1tkk, PDBe:1tkk, PDBj:1tkk
• PDBsum: 1tkk
• PubMed: 15301535
• UniProt: O34508|AEEP_BACSU L-Ala-D/L-Glu epimerase (Gene Name=ykfB)