Structure of PDB 1fbx Chain E Binding Site BS01

Receptor Information

>1fbx Chain E (length=221) Species: 562 (Escherichia coli)

PSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLL
NLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVT
VRDITLTSTCEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQV
QERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLG
GLFKSSQNTRHEFLRAVRHHN

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 1fbx Chain E Residue 3320

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1fbx Zinc plays a key role in human and bacterial GTP cyclohydrolase I.
• Resolution: 2.8 Å
• Binding residue (original residue number in PDB): C110 H113 C181
• Binding residue (residue number reindexed from 1): C110 H113 C181
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): C110 E111 H112 H113 Q151 H179 C181
• Catalytic site (residue number reindexed from 1): C110 E111 H112 H113 Q151 H179 C181
• Enzyme Commision number: 3.5.4.16: GTP cyclohydrolase I.

Gene Ontology

Molecular Function

• GO:0003934 GTP cyclohydrolase I activity
• GO:0005525 GTP binding
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006729 tetrahydrobiopterin biosynthetic process
• GO:0006730 one-carbon metabolic process
• GO:0008616 queuosine biosynthetic process
• GO:0046654 tetrahydrofolate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0032991 protein-containing complex

External links

• PDB: RCSB:1fbx, PDBe:1fbx, PDBj:1fbx
• PDBsum: 1fbx
• PubMed: 11087827
• UniProt: P0A6T5|GCH1_ECOLI GTP cyclohydrolase 1 (Gene Name=folE)