Structure of PDB 3kum Chain F

Receptor sequence
>3kumF (length=354) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
MKIKQVHVRASKIKLKETFTIALGTIESADSAIVEIETEEGLVGYGEGGP
GIFITGETLAGTLETIELFGQAIIGLNPFNIEKIHEVMDKISAFAPAAKA
AIDIACYDLMGQKAQLPLYQLLGGYDNQVITDITLGIDEPNVMAQKAVEK
VKLGFDTLKIKVGTGIEADIARVKAIREAVGFDIKLRLDANQAWTPKDAV
KAIQALADYQIELVEQPVKRRDLEGLKYVTSQVNTTIMADESCFDAQDAL
ELVKKGTVDVINIKLMKCGGIHEALKINQICETAGIECMIGCMAEETTIG
ITAAAHLAAAQKNITRADLDATFGLETAPVTGGVSLEAKPLLELGEAAGL
GISH
3D structure
PDB3kum Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
ChainF
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
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 ARG F F19 K161 C292 D318 D320 F19 K161 C292 D318 D320
BS02 TYR F I21 F53 I54 K161 D240 K264 A294 E295 I21 F53 I54 K161 D240 K264 A294 E295
BS03 MG F 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

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3kum, PDBe:3kum, PDBj:3kum
PDBsum3kum
PubMed22392983
UniProtQ834W6|HYEP_ENTFA Hydrophobic dipeptide epimerase (Gene Name=EF_1511)

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