Structure of PDB 3jzu Chain D

Receptor sequence

>3jzuD (length=354) Species: 226185 (Enterococcus faecalis V583)

MKIKQVHVRASKIKLKETFTIALGTIESADSAIVEIETEEGLVGYGEGGP
GIFITGETLAGTLETIELFGQAIIGLNPFNIEKIHEVMDKISAFAPAAKA
AIDIACYDLMGQKAQLPLYQLLGGYDNQVITDITLGIDEPNVMAQKAVEK
VKLGFDTLKIKVGTGIEADIARVKAIREAVGFDIKLRLDANQAWTPKDAV
KAIQALADYQIELVEQPVKRRDLEGLKYVTSQVNTTIMADESCFDAQDAL
ELVKKGTVDVINIKLMKCGGIHEALKINQICETAGIECMIGCMAEETTIG
ITAAAHLAAAQKNITRADLDATFGLETAPVTGGVSLEAKPLLELGEAAGL
GISH

3D structure

• PDB: 3jzu Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
• Chain: D
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F19 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): F19 P50 F53 T134 K159 K161 D189 N191 E215 D240 E241 S242 N262 K264 G291 C292 M293 A317 D318 L319
• 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	LEU	D	F19 K161 C292 A294 D318 D320 A321	F19 K161 C292 A294 D318 D320 A321
BS02	TYR	D	F53 K161 D240 K264 C292 M293 A294 E295	F53 K161 D240 K264 C292 M293 A294 E295
BS03	MG	D	D189 E215 D240	D189 E215 D240

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