MolNFT v1 · #171522 · protein
Human GTP cyclohydrolase I
6Z87 · GTP cyclohydrolase 1: “Human GTP cyclohydrolase I”. X-ray diffraction, 1 ligand (ZN), 20 pockets (best druggability 0.79). MolNFT v1 #171522 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Z87
- Type
- protein
- Length
- 934 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP cyclohydrolase 1
- EC
- 3.5.4.16
- UniProt
- P30793
- Ligands
- ZN
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 188 | 45% helix, 26% strand | P30793 |
| B | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 181 | 45% helix, 24% strand | P30793 |
| C | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 189 | 46% helix, 25% strand | P30793 |
Ligands and binding sites
- ZN · Zinc ion · metal · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 596 | 0.79 | 0.85 | 41 | empty |
| 2 | 103 | 0.64 | 0.89 | 25 | ZN |
| 3 | 125 | 0.62 | 0.86 | 26 | empty |
| 4 | 115 | 0.62 | 0.87 | 26 | empty |
| 5 | 129 | 0.58 | 0.84 | 30 | empty |
Interfaces
10 interfaces between chains.
- B–C · 1126 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1117 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1108 Ų buried · 19 hydrogen bonds · protein-protein
- A–E · 1075 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1036 Ų buried · 16 hydrogen bonds · protein-protein
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 P30793
- Elsewhere: RCSB PDB 6Z87 · PDBe 6Z87 · UniProt P30793
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