Structure of PDB 3gf0 Chain A Binding Site BS02

Receptor Information

>3gf0 Chain A (length=199) Species: 2190 (Methanocaldococcus jannaschii)

MILSDKDIIDYVTSKRIIIKPFNKDFVGPCSYDVTLGDEFIIYDDEVYDL
SKELNYKRIKIKNSILVCPLNYNLTEEKINYFKEKYNVDYVVEGGVLGTT
NEYIELPNDISAQYQGRSSLGRVFLTSHQTAGWIDAGFKGKITLQIVAFD
KPVILYKNQRIGQLIFSKLLSPADVGYSERKTSKYAYQKSVMPSLIHLD

Ligand information

• Ligand ID: POP
• InChI: InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-2
• InChIKey: XPPKVPWEQAFLFU-UHFFFAOYSA-L
• SMILES:
  OpenEye OEToolkits 1.5.0: O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
  CACTVS 3.341: O[P]([O-])(=O)O[P](O)([O-])=O
  ACDLabs 10.04: [O-]P(=O)(O)OP([O-])(=O)O
  OpenEye OEToolkits 1.5.0: OP(=O)([O-])OP(=O)(O)[O-]
• Formula: H2 O7 P2
• Name: PYROPHOSPHATE 2-
• PDB chain: 3gf0 Chain A Residue 277

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3gf0 Pre-steady State Kinetic and Structural Evidence for a Concerted Biofunctionality in dCTP deaminase-dUTPase from Methanocaldococcus jannaschii
• Resolution: 2.62 Å
• Binding residue (original residue number in PDB): Y177 S183 K184 Y185
• Binding residue (residue number reindexed from 1): Y177 S183 K184 Y185
• Annotation score: 5

Enzymatic activity

• Catalytic site (original residue number in PDB): S118 R122 A131 W133 Q145
• Catalytic site (residue number reindexed from 1): S118 R122 A131 W133 Q145
• Enzyme Commision number: 3.5.4.30: dCTP deaminase (dUMP-forming).

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0008829 dCTP deaminase activity
• GO:0016787 hydrolase activity
• GO:0033973 dCTP deaminase (dUMP-forming) activity

Biological Process

• GO:0006226 dUMP biosynthetic process
• GO:0006229 dUTP biosynthetic process
• GO:0009117 nucleotide metabolic process

External links

• PDB: RCSB:3gf0, PDBe:3gf0, PDBj:3gf0
• PDBsum: 3gf0
• UniProt: Q57872|DCDB_METJA dCTP deaminase, dUMP-forming (Gene Name=dcd)