Research workbench
MSRB3
Analyse MSRB3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q9V
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine-R-sulfoxide reductase B3
- EC
- 1.8.4.12, 1.8.4.14
- UniProt
- Q8IXL7
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine-R-sulfoxide reductase B3 (EC 1.8.4.12, 1.8.4.14) | protein | 142 | 20% helix, 27% strand | Q8IXL7 |
| B | Methionine-R-sulfoxide reductase B3 (EC 1.8.4.12, 1.8.4.14) | protein | 145 | 16% helix, 28% strand | Q8IXL7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.59 | 0.80 | 40 | MPD |
| 2 | 59 | 0.37 | 0.80 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 377 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 modified, 2 disulfide (methylation, disulfide, oxidation).
Compared structures
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 Q8IXL7
- Elsewhere: RCSB PDB 6Q9V · PDBe 6Q9V · UniProt Q8IXL7
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