Structure of PDB 6sbi Chain D

Receptor sequence
>6sbiD (length=216) Species: 10090 (Mus musculus) [Search protein sequence]
TKPLSRFWEWGKNIVCVGRNYADHVKEMRSTVLSEPVLFLKPSTAYAPEG
SPVLMPAYCRNLHHEVELGVLLGKRGEAIPEAAAMDYVAGYALCLDMTAR
DVQEECKKKGLPWTLAKSFTSSCPVSAFVPKEKIPDPHALRLWLKVNGEL
RQEGKTSSMIFSIPYIISYVSKIITLEEGDLILTGTPKGVGPIKENDEIE
AGIDGVVSMRFKVKRS
3D structure
PDB6sbi Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.
ChainD
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S52 T184 V199
Catalytic site (residue number reindexed from 1) S43 T175 V190
Enzyme Commision number 3.7.1.5: acylpyruvate hydrolase.
4.1.1.112: oxaloacetate decarboxylase.
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 MG D E74 E76 D105 E65 E67 D96
BS02 OXL D G27 H33 E74 E76 G194 T195 G18 H24 E65 E67 G185 T186
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008948 oxaloacetate decarboxylase activity
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0018773 acetylpyruvate hydrolase activity
GO:0034545 fumarylpyruvate hydrolase activity
GO:0046872 metal ion binding
GO:0047621 acylpyruvate hydrolase activity
GO:0050163 oxaloacetate tautomerase activity
Biological Process
GO:0006090 pyruvate metabolic process
GO:0006107 oxaloacetate metabolic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005759 mitochondrial matrix
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:6sbi, PDBe:6sbi, PDBj:6sbi
PDBsum6sbi
PubMed32068790
UniProtQ8R0F8|FAHD1_MOUSE Oxaloacetate tautomerase FAHD1, mitochondrial (Gene Name=Fahd1)

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