Research workbench
Crystal structure of GTP cyclohydrolase-ib with 8-oxo-GTP
Analyse Crystal structure of GTP cyclohydrolase-ib with 8-oxo-GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K95
- Type
- protein
- Length
- 490 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP cyclohydrolase FOLE2
- EC
- 3.5.4.16
- UniProt
- Q5F9K6
- Ligands
- 8GT, ZN
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GTP cyclohydrolase FOLE2 (EC 3.5.4.16) | protein | 245 | 24% helix, 44% strand | Q5F9K6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.70 | 0.93 | 24 | empty |
| 2 | 97 | 0.69 | 0.92 | 23 | empty |
| 3 | 111 | 0.48 | 0.80 | 28 | 8GT, ZN |
| 4 | 138 | 0.45 | 0.76 | 23 | empty |
| 5 | 79 | 0.33 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1785 Ų buried · 40 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
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 Q5F9K6
- Elsewhere: RCSB PDB 5K95 · PDBe 5K95 · UniProt Q5F9K6
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