Research workbench
Aquifex aeolicus mura in complex with udp-N-acetylmuramic acid and covalent adduct of pep with CYS124
Analyse Aquifex aeolicus mura in complex with udp-N-acetylmuramic acid and covalent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SWG
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O67315
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 417 | — | O67315 |
Compared structures
- 3SWG · AQUIFEX AEOLICUS MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP… · the same entry in another collection · chain A against A, TM-score 1.00
- O67315 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · 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 O67315
- Elsewhere: RCSB PDB 3SWG · PDBe 3SWG · UniProt O67315
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