Research workbench
Crystal structure of apo E. COLI GTP cyclohydrolase II
Analyse Crystal structure of apo E. COLI GTP cyclohydrolase II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BZ1
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP cyclohydrolase II
- EC
- 3.5.4.25
- UniProt
- P0A7I7
- Ligands
- TAU, ZN, SO4
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP cyclohydrolase II (EC 3.5.4.25) | protein | 173 | 35% helix, 29% strand | P0A7I7 |
Ligands and binding sites
- TAU · 2-aminoethanesulfonic acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.58 | 0.79 | 36 | SO4, TAU |
| 2 | 55 | 0.28 | 0.74 | 12 | empty |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0A7I7
- Elsewhere: RCSB PDB 2BZ1 · PDBe 2BZ1 · UniProt P0A7I7
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