Research workbench
Crystal structure of listeria monocytogenes GTP cyclohydrolase I
Analyse Crystal structure of listeria monocytogenes 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
- 4UQF
- Type
- protein
- Length
- 1,860 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP cyclohydrolase 1
- EC
- 3.5.4.16
- UniProt
- A0A1D2IZD1
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 186 | 45% helix, 25% strand | A0A1D2IZD1 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1132 | 0.82 | 0.83 | 174 | empty |
| 2 | 730 | 0.81 | 0.85 | 42 | empty |
| 3 | 252 | 0.79 | 0.91 | 33 | empty |
| 4 | 795 | 0.79 | 0.82 | 41 | empty |
| 5 | 743 | 0.78 | 0.82 | 114 | empty |
Interfaces
25 interfaces between chains.
- D–G · 2034 Ų buried · 15 hydrogen bonds · protein-protein
- E–I · 2012 Ų buried · 13 hydrogen bonds · protein-protein
- H–J · 2002 Ų buried · 13 hydrogen bonds · protein-protein
- A–F · 1988 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1986 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 4UQF · Crystal structure of listeria monocytogenes 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 A0A1D2IZD1
- Elsewhere: RCSB PDB 4UQF · PDBe 4UQF · UniProt A0A1D2IZD1
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