Structure of PDB 2v6k Chain A

Receptor sequence
>2v6kA (length=214) Species: 70356 (Ralstonia sp. U2) [Search protein sequence]
AKMKLYNFWRSGTSHRLRIALNLKGVPYEYLAVHLGKEEHLKDAFKALNP
QQLVPALDTGAQVLIQSPAIIEWLEEQYPTPALLPADADGRQRVRALAAI
VGCDIHPINNRRILEYLRKTFGADEAAINAWCGTWISAGFDAYEALLAVD
PKRGRYSFGDTPTLADCYLVPQVESARRFQVDLTPYPLIRAVDAACGELD
AFRRAAPAAQPDSA
3D structure
PDB2v6k Structure of Bacterial Glutathione-S-Transferase Maleyl Pyruvate Isomerase and Implications for Mechanism of Isomerisation.
ChainA
Resolution1.3 Å
3D
structure
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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 TGG A S9 G10 T11 H38 L51 V52 Q64 S65 H104 N108 R109 R110 S11 G12 T13 H40 L53 V54 Q66 S67 H106 N110 R111 R112
BS02 ACT A R109 E113 R111 E115
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2v6k, PDBe:2v6k, PDBj:2v6k
PDBsum2v6k
PubMed18824004
UniProtO86043|NAGL_RALSP Maleylpyruvate isomerase (Gene Name=nagL)

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