Research workbench
Crystal structure of imidazole glycerol phosphate synthase subunit hisf (ec 4.1.3.-) (TM1036) from thermotoga maritima at 1.64 a resolution
Analyse Crystal structure of imidazole glycerol phosphate synthase subunit hisf (ec… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A0N
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imidazole glycerol phosphate synthase subunit hisf
- EC
- 4.1.3.-
- UniProt
- Q9X0C6
- Ligands
- UNL, IOD, PO4
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Imidazole glycerol phosphate synthase subunit hisf (EC 4.1.3.-) | protein | 251 | 40% helix, 25% strand | Q9X0C6 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · chains A
- IOD · Iodide ion · ion · 7 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.63 | 0.78 | 45 | IOD, PO4, UNL |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2A0N · Crystal structure of Imidazole glycerol phosphate synthase subunit hisF (EC 4.1.3.-)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0C6 · AlphaFold monomer V2.0 prediction for imidazole glycerol phosphate synthase subunit hisf… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9X0C6
- Elsewhere: RCSB PDB 2A0N · PDBe 2A0N · UniProt Q9X0C6
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