Research workbench
Insights into function, catalytic mechanism and fold evolution of mouse selenoprotein methionine sulfoxide reductase B1 through structural analysis
Analyse Insights into function, catalytic mechanism and fold evolution of mouse… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KV1
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine-R-sulfoxide reductase B1
- EC
- 1.8.4.-
- UniProt
- Q9JLC3
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.69
Structure
solution nmr · 1 distinct chain · 2% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine-R-sulfoxide reductase B1 (EC 1.8.4.-) | protein | 124 | 2% helix, 20% strand | Q9JLC3 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
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 | 208 | 0.69 | 0.86 | 33 | empty |
| 2 | 307 | 0.55 | 0.75 | 37 | empty |
Compared structures
- 2KV1 · Insights into Function, Catalytic Mechanism and Fold Evolution of Mouse Selenoprotein… · 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 Q9JLC3
- Elsewhere: RCSB PDB 2KV1 · PDBe 2KV1 · UniProt Q9JLC3
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