Research workbench
Crystal structure of the Y361F mutant of staphylococcus aureus coadr
Analyse Crystal structure of the Y361F mutant of staphylococcus aureus coadr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EQR
- Type
- protein
- Length
- 874 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
- Q2FIA5
- Ligands
- COA, FAD, MG, CL
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Coenzyme a disulfide reductase (EC 1.8.1.14) | protein | 437 | 28% helix, 30% strand | Q2FIA5 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 3 copies · chains B
- CL · Chloride ion · ion · 6 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1122 | 0.83 | 0.84 | 117 | CL, COA, FAD |
| 2 | 1102 | 0.83 | 0.84 | 117 | CL, COA, FAD |
| 3 | 351 | 0.58 | 0.76 | 36 | empty |
| 4 | 97 | 0.45 | 0.79 | 20 | empty |
| 5 | 89 | 0.40 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2787 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 4EQR · Crystal structure of the Y361F mutant of Staphylococcus aureus CoADR · the same entry in another collection · chain A against A, TM-score 1.00
- Q2FIA5 · AlphaFold monomer V2.0 prediction for coenzyme a disulfide reductase (Q2FIA5) · a predicted model of the same protein · chain B 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 Q2FIA5
- Elsewhere: RCSB PDB 4EQR · PDBe 4EQR · UniProt Q2FIA5
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