Research workbench
Thiazole synthase from neurospora crassa
Analyse Thiazole synthase from neurospora crassa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JSK
- Type
- protein
- Length
- 4,662 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CYPBP37 protein
- UniProt
- Q9HGR2
- Ligands
- AHZ, FE2
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F, N, O | CYPBP37 protein | protein | 292 | 40% helix, 23% strand | Q9HGR2 |
| B, E, G, H, I, J, K, L, M, P | CYPBP37 protein | protein | 291 | 40% helix, 22% strand | Q9HGR2 |
Ligands and binding sites
- AHZ · Adenosine diphosphate 5-(beta-ethyl)-4-methyl-thiazole-2-carboxylic acid · ligand · 16 copies · chains A, F, B, H, C, D, E, G, I, N, J, P, K, L, M, O
- FE2 · Fe (II) ion · metal · 16 copies · chains A, F, B, H, C, D, E, G, I, N, J, P, K, O, L, M
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.86 | 0.88 | 101 | AHZ, FE2 |
| 2 | 980 | 0.86 | 0.87 | 106 | AHZ, FE2 |
| 3 | 1051 | 0.86 | 0.87 | 108 | AHZ, FE2 |
| 4 | 996 | 0.86 | 0.87 | 114 | AHZ, FE2 |
| 5 | 1003 | 0.86 | 0.87 | 109 | AHZ, FE2 |
Interfaces
40 interfaces between chains.
- E–F · 4049 Ų buried · 53 hydrogen bonds · protein-protein
- G–H · 4045 Ų buried · 52 hydrogen bonds · protein-protein
- J–K · 4033 Ų buried · 51 hydrogen bonds · protein-protein
- I–L · 4027 Ų buried · 47 hydrogen bonds · protein-protein
- B–C · 4015 Ų buried · 45 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (nonstandard).
Compared structures
- 3JSK · Thiazole synthase from Neurospora crassa · 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 Q9HGR2
- Elsewhere: RCSB PDB 3JSK · PDBe 3JSK · UniProt Q9HGR2
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