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Crystal Structure of Human Methionine-R-Sulfoxide Reductase B1 (MsrB1)
Analyse Crystal Structure of Human Methionine-R-Sulfoxide Reductase B1 (MsrB1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MAO
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.42
- Source
- Homo sapiens
- Molecule
- Methionine-R-sulfoxide reductase B1
- EC
- 1.8.4.-
- UniProt
- Q9NZV6
- Ligands
- NA, FE
Structure
x-ray diffraction · resolution 1.42 · 1 distinct chain · 6% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine-R-sulfoxide reductase B1 (EC 1.8.4.-) | protein | 105 | 6% helix, 37% strand | Q9NZV6 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A
- FE · Fe (III) ion · metal · chains A
- MLI · Malonate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3MAO · Crystal structure of human methionine-R-sulfoxide reductase B1 (MSRB1) · 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 Q9NZV6
- Elsewhere: RCSB PDB 3MAO · PDBe 3MAO · UniProt Q9NZV6
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