Structure of PDB 4hg3 Chain B

Receptor sequence
>4hg3B (length=303) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
LKRVAVAQLCSSADLTKNLKVVKELISEAIQKKADVVFLPEASDYLSQNP
LHSRYLAQKSPKFIRQLQSSITDLVRDNSRNIDVSIGVHLPPSEQDLLEG
NDRVRNVLLYIDHEGKILQEYQKLHLFDVDVPNGPILKESKSVQPGKAIP
DIIESPLGKLGSAICYDIRFPEFSLKLRSMGAEILCFPSAFTIKTGEAHW
ELLGRARAVDTQCYVLMPGQVGMHDLSDPEWEKQSHMSALEKSSRRESWG
HSMVIDPWGKIIAHADPSTVGPQLILADLDRELLQEIRNKMPLWNQRRDD
LFH
3D structure
PDB4hg3 Structures of enzyme-intermediate complexes of yeast Nit2: insights into its catalytic mechanism and different substrate specificity compared with mammalian Nit2
ChainB
Resolution1.93 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N110 K127 E143 C169 T196
Catalytic site (residue number reindexed from 1) N106 K123 E139 C165 T192
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 AKG B F131 C169 Y170 R173 F195 T199 F127 C165 Y166 R169 F191 T195
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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Biological Process
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Cellular Component
External links
PDB RCSB:4hg3, PDBe:4hg3, PDBj:4hg3
PDBsum4hg3
PubMed23897470
UniProtP47016|NIT2_YEAST Deaminated glutathione amidase (Gene Name=NIT2)

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