Research workbench
GTP cyclohydrolase I (C110S mutant) in complex with GTP
Analyse GTP cyclohydrolase I (C110S mutant) in complex with GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A9C
- 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 0.81
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 | 795 | 0.81 | 0.84 | 79 | empty |
| 2 | 616 | 0.78 | 0.84 | 56 | empty |
| 3 | 144 | 0.69 | 0.89 | 21 | empty |
| 4 | 174 | 0.69 | 0.88 | 24 | empty |
| 5 | 151 | 0.68 | 0.88 | 23 | empty |
Interfaces
16 interfaces between chains.
- G–H · 1310 Ų buried · 29 hydrogen bonds · protein-protein
- K–O · 1308 Ų buried · 25 hydrogen bonds · protein-protein
- M–N · 1303 Ų buried · 27 hydrogen bonds · protein-protein
- D–E · 1301 Ų buried · 27 hydrogen bonds · protein-protein
- K–L · 1299 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 1A9C · GTP cyclohydrolase I (C110S 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 1A9C · PDBe 1A9C · UniProt P0A6T5
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