MolNFT v1 · #15406 · protein
Biosynthesis of pteridins. reaction mechanism of GTP cyclohydrolase I
1N3T: “Biosynthesis of pteridins. reaction mechanism of GTP cyclohydrolase I”. X-ray diffraction, 1 ligand (GTP), 20 pockets (best druggability 0.85). MolNFT v1 #15406 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1N3T
- Type
- protein
- Length
- 3,315 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP cyclohydrolase I
- EC
- 3.5.4.16
- UniProt
- P0A6T5
- Ligands
- GTP
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, G, H, I, J, K, L, M, N, O, A, B, C, D, E | GTP cyclohydrolase I (EC 3.5.4.16) | protein | 221 | 44% helix, 22% strand | P0A6T5 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 15 copies · chains F, J, N, G, M, H, L, I, K, O, A, E, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 894 | 0.85 | 0.87 | 133 | empty |
| 2 | 177 | 0.81 | 0.96 | 41 | empty |
| 3 | 173 | 0.81 | 0.96 | 40 | empty |
| 4 | 177 | 0.81 | 0.96 | 42 | empty |
| 5 | 160 | 0.80 | 0.96 | 39 | empty |
Interfaces
30 interfaces between chains.
- J–N · 2491 Ų buried · 32 hydrogen bonds · protein-protein
- F–M · 2489 Ų buried · 32 hydrogen bonds · protein-protein
- G–L · 2487 Ų buried · 33 hydrogen bonds · protein-protein
- I–O · 2476 Ų buried · 30 hydrogen bonds · protein-protein
- H–K · 2454 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 1N3T · Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I · 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 P0A6T5
- Elsewhere: RCSB PDB 1N3T · PDBe 1N3T · UniProt P0A6T5
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