Structure of PDB 3rit Chain B

Receptor sequence
>3ritB (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.
ChainB
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 B Y19 T135 K160 K162 C294 D296 D321 Y19 T135 K160 K162 C294 D296 D321
BS02 DLY B Y19 K160 K162 D190 E216 D241 K266 M295 Y19 K160 K162 D190 E216 D241 K266 M295
BS03 MG B D190 E216 D241 E242 D190 E216 D241 E242
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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