Structure of PDB 3mkv Chain F

Receptor sequence
>3mkvF (length=413) Species: 32644 (unidentified) [Search protein sequence]
TTFLFRNGALLDPDHPDLLQGFEILIEDGFIREVSDKPIKSSNAHVIDVK
GKTIMPGLIDLHVHVVAIEFNLPRVATLPNVLVTLRAVPIMRAMLRRGFT
TVRDAGGAGYPFKQAVESGLVEGPRLFVSGRALSQTGGHADPRARSDYMP
PDSPCGCCVRVGALGRVADGVDEVRRAVREELQMGADQIKIMASGGVASP
TDPVGVFGYSEDEIRAIVAEAQGRGTYVLAHAYTPAAIARAVRCGVRTIE
HGNLIDDETARLVAEHGAYVVPTLVTYDALASEGEKYGLPPESIAKIADV
HGAGLHSIEIMKRAGVKMGFGTDLLGEAQRLQSDEFRILAEVLSPAEVIA
SATIVSAEVLGMQDKLGRIVPGAHADVLVVDGNPLKSVDCLLGQGEHIPL
VMKDGRLFVNELE
3D structure
PDB3mkv Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily .
ChainF
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 ZN F H63 H65 K191 D324 H62 H64 K190 D323
BS02 ZN F K191 H232 H252 K190 H231 H251
BS03 CO3 F H140 V198 A199 Y234 H139 V197 A198 Y233
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3mkv, PDBe:3mkv, PDBj:3mkv
PDBsum3mkv
PubMed20604542
UniProtB2T4I1

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