Structure of PDB 3n2c Chain H

Receptor sequence
>3n2cH (length=408) Species: 32644 (unidentified) [Search protein sequence]
TITVLQGGNVLDLERGVLLEHHHVVIDGERIVEVTDRPVDLPNAQAIDVR
GKTVMPGFIDCHVHVLASNANLGVNATQPNILAAIRSLPILDAMLSRGFT
SVRDAGGADWSLMQAVETGLVSGPRIFPSGKALSQTGGHGDFRPRGDLLE
PCSCCFRTGAIARVVDGVEGVRLAVREEIQKGATQIKIMASGGVASPTDP
IANTQYSEDEIRAIVDEAEAANTYVMAHAYTGRAIARAVRCGVRTIEHGN
LVDEAAAKLMHEHGAFVVPTLVTYDALAKHGAEFGMPPESVAKVASVQQK
GRESLEIYANAGVKMGFGSDLLGEMHAFQSGEFRIRAEVLGNLEALRSAT
TVAAEIVNMQGQLGVIAVGAIADLVVLDGNPLEDIGVVADEGARVEYVLQ
RGTLVKRQ
3D structure
PDB3n2c Functional identification and structure determination of two novel prolidases from cog1228 in the amidohydrolase superfamily .
ChainH
Resolution2.81 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 H H63 H65 K188 D321 H62 H64 K187 D320
BS02 ZN H K188 H229 H249 K187 H228 H248
BS03 LWY H H140 K188 V195 A196 H229 Y231 D321 L323 H139 K187 V194 A195 H228 Y230 D320 L322
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:3n2c, PDBe:3n2c, PDBj:3n2c
PDBsum3n2c
PubMed20604542
UniProtQ393A1

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