Structure of PDB 4hgd Chain A

Receptor sequence
>4hgdA (length=299) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
LKRVAVAQLCSSADLTKNLKVVKELISEAIQKKADVVFLPEASDYLSQNP
LHSRYLAQKSPKFIRQLQSSITDLVRDNSRNIDVSIGVHLPPSEQDLLEG
NDRVRNVLLYIDHEGKILQEYQKLHLFDVDVPNPILKESKSVQPGKAIPD
IIESPLGKLGSAISYDIRFPEFSLKLRSMGAEILCFPSAFTIKTGEAHWE
LLGRARAVDTQCYVLMPGQVGMHDLSDPEWEKQSHMSALEKRRESWGHSM
VIDPWGKIIAHADPSTVGPQLILADLDRELLQEIRNKMPLWNQRRDDLF
3D structure
PDB4hgd Structures of enzyme-intermediate complexes of yeast Nit2: insights into its catalytic mechanism and different substrate specificity compared with mammalian Nit2
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K127 S169
Catalytic site (residue number reindexed from 1) K123 S164
Enzyme Commision number 3.5.1.128: deaminated glutathione amidase.
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 KGT A E45 K127 F131 E143 S169 Y170 R173 A194 F195 T199 R250 E41 K123 F127 E138 S164 Y165 R168 A189 F190 T194 R243
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0050406 [acetyl-CoA carboxylase]-phosphatase activity
GO:0110050 deaminated glutathione amidase activity
Biological Process
GO:0043605 amide catabolic process
Cellular Component
GO:0005575 cellular_component
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4hgd, PDBe:4hgd, PDBj:4hgd
PDBsum4hgd
PubMed23897470
UniProtP47016|NIT2_YEAST Deaminated glutathione amidase (Gene Name=NIT2)

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