Research workbench
Pyrococcus horikoshii CoA disulfide reductase quadruple mutant
Analyse Pyrococcus horikoshii CoA disulfide reductase quadruple mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L1N
- Type
- protein
- Length
- 885 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coenzyme a disulfide reductase
- EC
- 1.8.1.14
- UniProt
- O58308
- Ligands
- FAD, COA
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coenzyme a disulfide reductase (EC 1.8.1.14) | protein | 442 | 28% helix, 30% strand | O58308 |
| B | Coenzyme a disulfide reductase (EC 1.8.1.14) | protein | 443 | 28% helix, 30% strand | O58308 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- COA · Coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.83 | 0.84 | 120 | FAD, COA |
| 2 | 1011 | 0.83 | 0.84 | 125 | FAD, COA |
| 3 | 94 | 0.56 | 0.85 | 16 | empty |
| 4 | 233 | 0.55 | 0.78 | 28 | empty |
| 5 | 116 | 0.53 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2843 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5L1N · Pyrococcus horikoshii CoA Disulfide Reductase Quadruple Mutant · the same entry in another collection · chain A against A, TM-score 1.00
- O58308 · AlphaFold monomer V2.0 prediction for NAD(P)H coenzyme a POLYSULFIDE/PERSULFIDE reductase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O58308
- Elsewhere: RCSB PDB 5L1N · PDBe 5L1N · UniProt O58308
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