Research workbench
Structure of 6-pyruvoyltetrahydropterin synthase
Analyse Structure of 6-pyruvoyltetrahydropterin synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QN0
- Type
- protein
- Length
- 702 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- EC
- 4.1.2.50
- UniProt
- C6EJA7
- Ligands
- ZN
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | 6-carboxy-5,6,7,8-tetrahydropterin synthase (EC 4.1.2.50) | protein | 117 | 31% helix, 36% strand | C6EJA7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 767 | 0.75 | 0.79 | 81 | empty |
| 2 | 397 | 0.73 | 0.84 | 62 | ZN |
| 3 | 276 | 0.62 | 0.80 | 30 | empty |
| 4 | 132 | 0.61 | 0.85 | 25 | ZN |
| 5 | 154 | 0.61 | 0.85 | 30 | empty |
Interfaces
9 interfaces between chains.
- D–E · 749 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 744 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 740 Ų buried · 13 hydrogen bonds · protein-protein
- C–E · 738 Ų buried · 19 hydrogen bonds · protein-protein
- B–F · 731 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3QN0 · Structure of 6-pyruvoyltetrahydropterin synthase · the same entry in another collection · chain A against A, TM-score 1.00
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 C6EJA7
- Elsewhere: RCSB PDB 3QN0 · PDBe 3QN0 · UniProt C6EJA7
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