Research workbench
Biosynthesis of pteridins. reaction mechanism of GTP cyclohydrolase I
Analyse Biosynthesis of pteridins. reaction mechanism of GTP cyclohydrolase I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N3R
- Type
- protein
- Length
- 3,314 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 0.78
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F, G, H, I, J, K, L, M, N, O | GTP cyclohydrolase I (EC 3.5.4.16) | protein | 221 | 44% helix, 21% strand | P0A6T5 |
| E | GTP cyclohydrolase I (EC 3.5.4.16) | protein | 220 | 40% helix, 21% strand | P0A6T5 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 15 copies · chains A, E, B, C, D, F, J, G, H, I, K, O, L, M, N
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 | 294 | 0.78 | 0.90 | 42 | empty |
| 2 | 547 | 0.74 | 0.82 | 56 | empty |
| 3 | 485 | 0.73 | 0.82 | 54 | empty |
| 4 | 101 | 0.69 | 0.92 | 18 | empty |
| 5 | 190 | 0.69 | 0.87 | 33 | empty |
Interfaces
16 interfaces between chains.
- A–B · 1268 Ų buried · 28 hydrogen bonds · protein-protein
- M–N · 1247 Ų buried · 27 hydrogen bonds · protein-protein
- F–G · 1242 Ų buried · 29 hydrogen bonds · protein-protein
- C–D · 1237 Ų buried · 29 hydrogen bonds · protein-protein
- K–L · 1236 Ų buried · 29 hydrogen bonds · protein-protein
Compared structures
- 1N3R · Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I · the same entry in another collection · chain C against C, 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 1N3R · PDBe 1N3R · UniProt P0A6T5
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