Research workbench
Crystal structure of a clostridial dehydrogenase at 2.55 angstroems resolution
Analyse Crystal structure of a clostridial dehydrogenase at 2.55 angstroems resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FZI
- Type
- protein
- Length
- 1,326 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q0STD4
- Ligands
- NAD
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 331 | — | Q0STD4 |
| B, D | — | protein | 332 | — | Q0STD4 |
| C | — | protein | 331 | — | Q0STD4 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 11 copies · chains A, C, B, D
- ACT · Acetate ion · additive · 9 copies · chains A, B, C, D
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q0STD4
- Elsewhere: RCSB PDB 6FZI · PDBe 6FZI · UniProt Q0STD4
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