Structure of PDB 3feq Chain L

Receptor sequence
>3feqL (length=404) Species: 32644 (unidentified) [Search protein sequence]
TITVLQGGNVLDLERGVLLEHHHVVIDGERIVEVTDRPVDLPNAQAIDVR
GKTVMPGFIDCHVHVLASNANLGVNATQPNILAAIRSLPILDAMLSRGFT
SVRDAGGADWSLMQAVETGLVSGPRIFPSGKALSQTGGHGDFRPREPCSC
CFRTGAIARVVDGVEGVRLAVREEIQKGATQIKIMASGGVASPTDPIANT
QYSEDEIRAIVDEAEAANTYVMAHAYTGRAIARAVRCGVRTIEHGNLVDE
AAAKLMHEHGAFVVPTLVTYDALAKHGAEFGMPPESVAKVASVQQKGRES
LEIYANAGVKMGFGSDLLGEMHAFQSGEFRIRAEVLGNLEALRSATTVAA
EIVNMQGQLGVIAVGAIADLVVLDGNPLEDIGVVADEGARVEYVLQRGTL
VKRQ
3D structure
PDB3feq Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily .
ChainL
Resolution2.63 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 L H63 H65 D321 H62 H64 D316
BS02 ZN L H229 H249 H224 H244
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
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:3feq, PDBe:3feq, PDBj:3feq
PDBsum3feq
PubMed20604542
UniProtQ393A1

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