MolNFT v1 · #144615 · protein
1.83 ångström resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with FAD.
6BZ0: “1.83 ångström resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in…”. X-ray diffraction, 3 ligands (FAD, MG, CL). MolNFT v1 #144615 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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