Structure of PDB 5ti1 Chain G

Receptor sequence
>5ti1G (length=429) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
ASSDLQATLDPSRKSWVESANNPTGDFSIQNLPFGIFSDGLNATRRVGVA
IGDSIVDLAALESAGLLSVPDSVFVRDALNDFIALGRDAWRSVRVQLSRL
LSRDDATLRDDAELRGRALIRQADAQLHLPVQIPGYTDFYSSKEHATNVG
SMFRDPKNALLPNWSEMPIGYNGRASSVVVSGTPVRRPNGQLKLPDQERP
VFGACRKLDIELETGFVIGAGNALGEPVTCADAEAHIFGMVLLNDWSARD
IQQWEYVPLGPFNAKTFATTISPWIVTLDALEPFRVAQPAQDPQPLAYLR
HDGEHAFDITLEVTLRPQQAKEASTITRTNFKHMYWTMAQQLAHHTVSGC
NTRVGDLMGSGTISGPTEDSFGSLLELTWNGKKPLELREGGTRSFIEDGD
ELTLAGWCQGEGYRVGFGVCAGEILPALK
3D structure
PDB5ti1 Crystal Structure of Fumarylacetoacetate hydrolase from Burkholderia xenovorans LB400
ChainG
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D145 H152 E218 E220 D252 R256 Q259 K272 T276 E383
Catalytic site (residue number reindexed from 1) D138 H145 E211 E213 D245 R249 Q252 K265 T269 E376
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 MG G D145 E218 E220 D252 D138 E211 E213 D245
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004334 fumarylacetoacetase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006559 L-phenylalanine catabolic process
GO:0006572 tyrosine catabolic process
GO:0009072 aromatic amino acid metabolic process
GO:1902000 homogentisate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ti1, PDBe:5ti1, PDBj:5ti1
PDBsum5ti1
PubMed
UniProtQ144Z1

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