Research workbench
1.83 ångström resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with FAD.
Analyse 1.83 ångström resolution crystal structure of dihydrolipoyl dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BZ0
- Type
- protein
- Length
- 1,875 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D0CDT4
- Ligands
- FAD, MG, CL
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 469 | — | D0CDT4 |
| C | — | protein | 468 | — | D0CDT4 |
| D | — | protein | 469 | — | D0CDT4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 2 copies
- CL · Chloride ion · ion · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BZ0 · 1.83 Angstrom Resolution Crystal Structure of Dihydrolipoyl Dehydrogenase from… · 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 D0CDT4
- Elsewhere: RCSB PDB 6BZ0 · PDBe 6BZ0 · UniProt D0CDT4
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