Structure of PDB 3jva Chain G

Receptor sequence

>3jvaG (length=345) Species: 226185 (Enterococcus faecalis V583)

MKIKQVHVRASKIKLKETSADSAIVEIETEEGLVGYGEGGPGIFITGETL
AGTLETIELFGQAIIGLNPFNIEKIHEVMDKISAFAPAAKAAIDIACYDL
MGQKAQLPLYQLLGGYDNQVITDITLGIDEPNVMAQKAVEKVKLGFDTLK
IKVGTGIEADIARVKAIREAVGFDIKLRLDANQAWTPKDAVKAIQALADY
QIELVEQPVKRRDLEGLKYVTSQVNTTIMADESCFDAQDALELVKKGTVD
VINIKLMKCGGIHEALKINQICETAGIECMIGCMAEETTIGITAAAHLAA
AQKNITRADLDATFGLETAPVTGGVSLEAKPLLELGEAAGLGISH

3D structure

• PDB: 3jva Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
• Chain: G
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): P50 F53 T134 K159 K161 D189 N191 E215 D240 E241 S242 N262 K264 G291 C292 M293 A317 D318 L319
• Catalytic site (residue number reindexed from 1): P41 F44 T125 K150 K152 D180 N182 E206 D231 E232 S233 N253 K255 G282 C283 M284 A308 D309 L310
• Enzyme Commision number: 5.1.1.-

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	G	D189 E215 D240	D180 E206 D231

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• 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

Biological Process

• GO:0006518 peptide metabolic process
• GO:0009063 amino acid catabolic process

External links

• PDB: RCSB:3jva, PDBe:3jva, PDBj:3jva
• PDBsum: 3jva
• PubMed: 22392983
• UniProt: Q834W6|HYEP_ENTFA Hydrophobic dipeptide epimerase (Gene Name=EF_1511)