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BioLiP

Structure of PDB 1qqj Chain A

Receptor sequence
>1qqjA (length=416) Species: 10090 (Mus musculus) [Search protein sequence]
MSFIPVAEDSDFPIQNLPYGVFSTQSNPKPRIGVAIGDQILDLSVIKHLF
TGPALSKHQHVFDETTLNNFMGLGQAAWKEARASLQNLLSASQARLRDDK
ELRQRAFTSQASATMHLPATIGDYTDFYSSRQHATNVGIMFRGKENALLP
NWLHLPVGYHGRASSIVVSGTPIRRPMGQMRPDNSKPPVYGACRLLDMEL
EMAFFVGPGNRFGEPIPISKAHEHIFGMVLMNDWSARDIQQWEYVPLGPF
LGKSFGTTISPWVVPMDALMPFVVPNPKQDPKPLPYLCHSQPYTFDINLS
VSLKGEGMSQAATICRSNFKHMYWTMLQQLTHHSVNGCNLRPGDLLASGT
ISGSDPESFGSMLELSWKGTKAIDVGQGQTRTFLLDGDEVIITGHCQGDG
YRVGFGQCAGKVLPAL
3D structure
PDB1qqj Crystal structure and mechanism of a carbon-carbon bond hydrolase.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D126 H133 E199 E201 D233 R237 Q240 K253 T257 E364
Catalytic site (residue number reindexed from 1) D126 H133 E199 E201 D233 R237 Q240 K253 T257 E364
Enzyme Commision number 3.7.1.2: fumarylacetoacetase.
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 CA A D126 E199 E201 D233 D126 E199 E201 D233
BS02 ACT A Y128 V137 R142 Y128 V137 R142
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004334 fumarylacetoacetase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006527 arginine catabolic process
GO:0006559 L-phenylalanine catabolic process
GO:0006572 tyrosine catabolic process
GO:0006629 lipid metabolic process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1qqj, PDBe:1qqj, PDBj:1qqj
PDBsum1qqj
PubMed10508789
UniProtP35505|FAAA_MOUSE Fumarylacetoacetase (Gene Name=Fah)

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