MolNFT v1 · #524 · protein
GTP cyclohydrolase I (H112S mutant) in complex with GTP
1A8R: “GTP cyclohydrolase I (H112S mutant) in complex with GTP”. X-ray diffraction, 1 ligand (GTP), 20 pockets (best druggability 0.86). MolNFT v1 #524 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1A8R
- 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 0.86
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, 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 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 15 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
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 | 1194 | 0.86 | 0.87 | 124 | empty |
| 2 | 1173 | 0.86 | 0.87 | 122 | empty |
| 3 | 995 | 0.85 | 0.87 | 102 | empty |
| 4 | 187 | 0.73 | 0.90 | 36 | empty |
| 5 | 177 | 0.73 | 0.91 | 29 | empty |
Interfaces
16 interfaces between chains.
- F–J · 1295 Ų buried · 33 hydrogen bonds · protein-protein
- I–J · 1291 Ų buried · 35 hydrogen bonds · protein-protein
- G–H · 1285 Ų buried · 33 hydrogen bonds · protein-protein
- C–D · 1284 Ų buried · 31 hydrogen bonds · protein-protein
- K–L · 1282 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 1A8R · GTP cyclohydrolase I (H112S mutant) in complex with GTP · the same entry in another collection · chain N against N, 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 1A8R · PDBe 1A8R · UniProt P0A6T5
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