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Crystal structure of azotobacter vinelandii L-rhamnose 1- DEHYDROGENASE(APO-form)
Analyse Crystal structure of azotobacter vinelandii L-rhamnose 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DO5
- Type
- protein
- Length
- 2,059 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- C1DMX5
- Ligands
- SO4
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 256 | — | C1DMX5 |
| B | — | protein | 261 | — | C1DMX5 |
| D, F | — | protein | 257 | — | C1DMX5 |
| E | — | protein | 248 | — | C1DMX5 |
| G | — | protein | 266 | — | C1DMX5 |
| H | — | protein | 258 | — | C1DMX5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 24 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7DO5 · Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase(apo-form) · 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 C1DMX5
- Elsewhere: RCSB PDB 7DO5 · PDBe 7DO5 · UniProt C1DMX5
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