Structure of PDB 3ro6 Chain A

Receptor sequence
>3ro6A (length=345) Species: 414 (Methylococcus capsulatus) [Search protein sequence]
MKIADIQVRTEHFPLTEEIDNLIVEIRTADGLLGLGAASPERHVTGETLE
ACHAALDHDRLGWLMGRDIRTLPRLCRELAERLPAAPAARAALDMALHDL
VAQCLGLPLVEILGRAHDSLPTSVTIGIKPVEETLAEAREHLALGFRVLK
VKLCGDEEQDFERLRRLHETLAGRAVVRVDPNQSYDRDGLLRLDRLVQEL
GIEFIEQPFPAGRTDWLRALPKAIRRRIAADESLLGPADAFALAAPPAAC
GIFNIKLMKCGGLAPARRIATIAETAGIDLMWGCMDESRISIAAALHAAL
ACPATRYLDLDGSFDLARDVAEGGFILEDGRLRVTERPGLGLVYP
3D structure
PDB3ro6 Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P50 H53 T135 K160 K162 D190 N192 E216 D241 E242 S243 K266 G293 C294 M295 L318 D319 L320
Catalytic site (residue number reindexed from 1) P40 H43 T125 K150 K152 D180 N182 E206 D231 E232 S233 K256 G283 C284 M285 L308 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 A D190 E216 D241 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

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Molecular Function
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Biological Process
External links
PDB RCSB:3ro6, PDBe:3ro6, PDBj:3ro6
PDBsum3ro6
PubMed22392983
UniProtQ607C7|KRDE_METCA L-Lys-D/L-Arg epimerase (Gene Name=MCA1834)

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