Structure of PDB 3rit Chain D

Receptor sequence
>3ritD (length=354) Species: 414 (Methylococcus capsulatus) [Search protein sequence]
MKIADIQVRTEHFPLTRPYRIAFRSIEEIDNLIVEIRTADGLLGLGAASP
ERHVTGETLEACHAALDHDRLGWLMGRDIRTLPRLCRELAERLPAAPAAR
AALDMALHDLVAQCLGLPLVEILGRAHDSLPTSVTIGIKPVEETLAEARE
HLALGFRVLKVKLCGDEEQDFERLRRLHETLAGRAVVRVDPNQSYDRDGL
LRLDRLVQELGIEFIEQPFPAGRTDWLRALPKAIRRRIAADESLLGPADA
FALAAPPAACGIFNIKLMKCGGLAPARRIATIAETAGIDLMWGCMDESRI
SIAAALHAALACPATRYLDLDGSFDLARDVAEGGFILEDGRLRVTERPGL
GLVY
3D structure
PDB3rit Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
ChainD
Resolution2.701 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 D Y19 T135 K162 D296 D319 D321 Y19 T135 K162 D296 D319 D321
BS02 DLY D E51 K160 K162 D190 E216 D241 K266 M295 E51 K160 K162 D190 E216 D241 K266 M295
BS03 MG D D190 E216 D241 D190 E216 D241
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

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Biological Process
External links
PDB RCSB:3rit, PDBe:3rit, PDBj:3rit
PDBsum3rit
PubMed22392983
UniProtQ607C7|KRDE_METCA L-Lys-D/L-Arg epimerase (Gene Name=MCA1834)

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