MolNFT v1 · #52602 · protein
Structure-based mechanism of lipoteichoic acid synthesis by staphylococcus aureus ltas.
2W5Q: “Structure-based mechanism of lipoteichoic acid synthesis by staphylococcus aureus ltas.”. X-ray diffraction. MolNFT v1 #52602 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2W5Q
- Type
- protein
- Length
- 424 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q7A1I3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 424 | — | Q7A1I3 |
Compared structures
- 2W5Q · Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS. · the same entry in another collection · chain A against A, TM-score 1.00
- Q7A1I3 · AlphaFold monomer V2.0 prediction for lipoteichoic acid synthase (Q7A1I3) · a predicted model of the same protein · 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 Q7A1I3
- Elsewhere: RCSB PDB 2W5Q · PDBe 2W5Q · UniProt Q7A1I3
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