Structure of PDB 2jl4 Chain A

Receptor sequence
>2jl4A (length=212) Species: 70356 (Ralstonia sp. U2) [Search protein sequence]
MKLYNFWRSGTSHRLRIALNLKGVPYEYLAVHLGKEEHLKDAFKALNPQQ
LVPALDTGAQVLIQSPAIIEWLEEQYPTPALLPADADGRQRVRALAAIVG
CDIHPINNRRILEYLRKTFGADEAAINAWCGTWISAGFDAYEALLAVDPK
RGRYSFGDTPTLADCYLVPQVESARRFQVDLTPYPLIRAVDAACGELDAF
RRAAPAAQPDSA
3D structure
PDB2jl4 Structure of Bacterial Glutathione-S-Transferase Maleyl Pyruvate Isomerase and Implications for Mechanism of Isomerisation.
ChainA
Resolution2.3 Å
3D
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Enzymatic activity
Enzyme Commision number 5.2.1.4: maleylpyruvate isomerase.
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 GSH A S9 T11 H38 L51 V52 Q64 S65 H104 N108 R109 R110 S9 T11 H38 L51 V52 Q64 S65 H104 N108 R109 R110
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004364 glutathione transferase activity
GO:0016034 maleylacetoacetate isomerase activity
GO:0016853 isomerase activity
GO:0050077 maleylpyruvate isomerase activity
Biological Process
GO:0006559 L-phenylalanine catabolic process
GO:0006749 glutathione metabolic process
GO:0009056 catabolic process
GO:0009072 aromatic amino acid metabolic process
GO:1901170 naphthalene catabolic process
Cellular Component
GO:0005737 cytoplasm

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External links
PDB RCSB:2jl4, PDBe:2jl4, PDBj:2jl4
PDBsum2jl4
PubMed18824004
UniProtO86043|NAGL_RALSP Maleylpyruvate isomerase (Gene Name=nagL)

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