Structure of PDB 5ti1 Chain A Binding Site BS01

Receptor Information

>5ti1 Chain A (length=426) Species: 266265 (Paraburkholderia xenovorans LB400)

SSDLQATLDPSRKSWVESANNPTGDFSIQNLPFGIFSDGLNATRRVGVAI
GDSIVDLAALESAGLLSVPDSVFVRDALNDFIALGRDAWRSVRVQLSRLL
SRDDATLRDDAELRGRALIRQADAQLHLPVQIPGYTDFYSSKEHATNVGS
MFRDNALLPNWSEMPIGYNGRASSVVVSGTPVRRPNGQLKLPDQERPVFG
ACRKLDIELETGFVIGAGNALGEPVTCADAEAHIFGMVLLNDWSARDIQQ
WEYVPLGPFNAKTFATTISPWIVTLDALEPFRVAQPAQDPQPLAYLRHDG
EHAFDITLEVTLRPQQAKEASTITRTNFKHMYWTMAQQLAHHTVSGCNTR
VGDLMGSGTISGPTEDSFGSLLELTWNGKKPLELREGGTRSFIEDGDELT
LAGWCQGEGYRVGFGVCAGEILPALK

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5ti1 Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5ti1 Crystal Structure of Fumarylacetoacetate hydrolase from Burkholderia xenovorans LB400
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D145 E218 E220 D252
• Binding residue (residue number reindexed from 1): D137 E208 E210 D242
• Annotation score: 1

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): D137 H144 E208 E210 D242 R246 Q249 K262 T266 E373
• Enzyme Commision number: 3.7.1.2: fumarylacetoacetase.

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

External links

• PDB: RCSB:5ti1, PDBe:5ti1, PDBj:5ti1
• PDBsum: 5ti1
• UniProt: Q144Z1