Research workbench
Human GTP cyclohydrolase I in complex with allosteric inhibitor
Analyse Human GTP cyclohydrolase I in complex with allosteric inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z89
- Type
- protein
- Length
- 821 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
- QBK, ZN
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 5 distinct chains · 44% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 181 | 46% helix, 27% strand | P30793 |
| B | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 173 | 45% helix, 26% strand | P30793 |
| C | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 120 | 35% helix, 42% strand | P30793 |
| D | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 180 | 46% helix, 27% strand | P30793 |
| E | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 167 | 46% helix, 26% strand | P30793 |
Ligands and binding sites
- QBK · 5-azanyl-[1,3]thiazolo[5,4-d]pyrimidine-2,7-dione · ligand · 2 copies · chains A, B, D, E
- 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
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 884 | 0.77 | 0.80 | 76 | empty |
| 2 | 57 | 0.59 | 0.91 | 21 | ZN |
| 3 | 71 | 0.53 | 0.86 | 23 | empty |
| 4 | 104 | 0.48 | 0.80 | 20 | ZN |
| 5 | 152 | 0.48 | 0.77 | 20 | QBK |
Interfaces
7 interfaces between chains.
- C–D · 1072 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1062 Ų buried · 18 hydrogen bonds · protein-protein
- A–E · 1018 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 968 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 950 Ų buried · 15 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 6Z89 · PDBe 6Z89 · UniProt P30793
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