Research workbench
Crystal structure of rhodanese-like domain protein from staphylococcus aureus
Analyse Crystal structure of rhodanese-like domain protein from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IWH
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rhodanese-like domain protein
- UniProt
- Q5HF17
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhodanese-like domain protein | protein | 102 | 36% helix, 20% strand | Q5HF17 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified, 1 covalent (engineered, additive adduct).
Compared structures
- 3IWH · Crystal Structure of Rhodanese-like Domain Protein from Staphylococcus aureus · 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 Q5HF17
- Elsewhere: RCSB PDB 3IWH · PDBe 3IWH · UniProt Q5HF17
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