Research workbench
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of gs-1
Analyse B. subtilis glutamine synthetase structures reveal large active site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LNO
- Type
- protein
- Length
- 2,664 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12425
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 444 | — | P12425 |
Compared structures
- 4LNO · B. subtilis glutamine synthetase structures reveal large active site conformational… · the same entry in another collection · chain C against C, TM-score 1.00
- P12425 · AlphaFold monomer V2.0 prediction for glutamine synthetase (P12425) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P12425
- Elsewhere: RCSB PDB 4LNO · PDBe 4LNO · UniProt P12425
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