Research workbench
Structure of bacterial cellulose synthase with cyclic-di-gmp bound.
Analyse Structure of bacterial cellulose synthase with cyclic-di-gmp bound. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P02
- Type
- protein
- Length
- 1,392 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q3J125, Q3J126
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 728 | — | Q3J125 |
| B | — | protein | 655 | — | Q3J126 |
| D | — | protein | 9 | — | — |
Compared structures
- 4P02 · Structure of Bacterial Cellulose Synthase with cyclic-di-GMP bound. · 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 Q3J125
- Every structure of UniProt Q3J126
- Elsewhere: RCSB PDB 4P02 · PDBe 4P02 · UniProt Q3J125 · UniProt Q3J126
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