Research workbench
Crystal structure of subhisa from the thermophile corynebacterium efficiens
Analyse Crystal structure of subhisa from the thermophile corynebacterium efficiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AXK
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-(5-phosphoribosyl)-5-((5'-phosphoribosylamino) METHYLIDENEAMINO)IMIDAZOLE-4-carboxamide…
- EC
- 5.3.1.16
- UniProt
- C8NPV3
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-(5-phosphoribosyl)-5-((5'-phosphoribosylamino) METHYLIDENEAMINO)IMIDAZOLE-4-carboxamide isomerase (EC 5.3.1.16) | protein | 235 | 43% helix, 25% strand | C8NPV3 |
| B | 1-(5-phosphoribosyl)-5-((5'-phosphoribosylamino) METHYLIDENEAMINO)IMIDAZOLE-4-carboxamide isomerase (EC 5.3.1.16) | protein | 239 | 41% helix, 23% strand | C8NPV3 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 878 | 0.73 | 0.77 | 65 | empty |
| 2 | 725 | 0.67 | 0.75 | 68 | empty |
Interfaces
1 interface between chains.
- A–B · 569 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4AXK · CRYSTAL STRUCTURE OF subHisA from the thermophile Corynebacterium efficiens · 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 C8NPV3
- Elsewhere: RCSB PDB 4AXK · PDBe 4AXK · UniProt C8NPV3
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