Research workbench
Structure of the E192N mutant of E. COLI N-acetylneuraminic acid lyase in space group P21
Analyse Structure of the E192N mutant of E. COLI N-acetylneuraminic acid lyase in space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WNQ
- Type
- protein
- Length
- 1,186 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6L4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | P0A6L4 |
| B | — | protein | 294 | — | P0A6L4 |
| C | — | protein | 296 | — | P0A6L4 |
| D | — | protein | 297 | — | P0A6L4 |
Compared structures
- 2WNQ · Structure of the E192N mutant of E. coli N-acetylneuraminic acid lyase in space group P21 · the same entry in another collection · chain D against D, TM-score 1.00
- P0A6L4 · AlphaFold monomer V2.0 prediction for N-acetylneuraminate lyase (P0A6L4) · a predicted model of the same protein · chain C 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 P0A6L4
- Elsewhere: RCSB PDB 2WNQ · PDBe 2WNQ · UniProt P0A6L4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.