Research workbench
Crystal structure of bovine peptide methionine sulfoxide reductase
Analyse Crystal structure of bovine peptide methionine sulfoxide reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FVG
- Type
- protein
- Length
- 192 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide methionine sulfoxide reductase
- EC
- 1.8.4.6
- UniProt
- P54149
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide methionine sulfoxide reductase (EC 1.8.4.6) | protein | 192 | 29% helix, 19% strand | P54149 |
Ligands and binding sites
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.29 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 3 modified, 2 covalent (engineered, additive adduct).
Compared structures
- 1FVG · Crystal structure of bovine peptide methionine sulfoxide reductase · the same entry in another collection · chain A against A, TM-score 1.00
- P54149 · AlphaFold monomer V2.0 prediction for mitochondrial peptide methionine sulfoxide… · a predicted model of the same protein · chain A 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 P54149
- Elsewhere: RCSB PDB 1FVG · PDBe 1FVG · UniProt P54149
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