MolNFT v1 · #70096 · protein
Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 ångströms resolution. a comparison with the structure of glutathione reductase
3LAD: “Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 ångströms resolution.…”. X-ray diffraction. MolNFT v1 #70096 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LAD
- Type
- protein
- Length
- 944 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P18925
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 472 | — | P18925 |
Compared structures
- 3LAD · Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2… · the same entry in another collection · chain A against A, TM-score 1.00
- P18925 · AlphaFold monomer V2.0 prediction for dihydrolipoyl dehydrogenase (P18925) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P18925
- Elsewhere: RCSB PDB 3LAD · PDBe 3LAD · UniProt P18925
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