Structure of PDB 3r0u Chain A

Receptor sequence
>3r0uA (length=362) Species: 484022 (Francisella philomiragia subsp. philomiragia ATCC 25017) [Search protein sequence]
VSKIIDIKTSIIKIPLKRTFITAVRSTNHIDSLAVELTLDNGVKGYGVAP
ATTAITGDTLQGMQYIIREIFAPVILGSDLSDYKQTLELAFKKVMFNSAA
KMAIDLAYHDLLAKEQDISVAKLLGAKANSIVTDVSISCGNVAETIQNIQ
NGVEANFTAIKVKTGADFNRDIQLLKALDNEFSKNIKFRFDANQGWNLAQ
TKQFIEEINKYSLNVEIIEQPVKYYDIKAMAEITKFSNIPVVADESVFDA
KDAERVIDEQACNMINIKLAKTGGILEAQKIKKLADSAGISCMVGCMMES
PAGILATASFALAEDITVADLDPLDWVAKDLYSDYITFNEPNIILKDNLK
GFGFNLAENLYF
3D structure
PDB3r0u Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F21 A52 A55 S137 K162 K164 D192 N194 E220 D245 E246 S247 K269 G296 C297 M298 D321
Catalytic site (residue number reindexed from 1) F20 A51 A54 S136 K161 K163 D191 N193 E219 D244 E245 S246 K268 G295 C296 M297 D320
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 D192 E220 D245 D191 E219 D244
BS02 MG A T235 S238 T234 S237
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3r0u, PDBe:3r0u, PDBj:3r0u
PDBsum3r0u
PubMed22392983
UniProtB0TZW0|XEEP_FRAP2 L-amino acid-D/L-Glu epimerase (Gene Name=Fphi_1647)

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