MolNFT v1 · #148922 · protein
Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct C-terminal arm (recombinant protein with shortened C-terminal, ADH508)
6FKV: “Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an…”. X-ray diffraction, 2 ligands (SO4, CL). MolNFT v1 #148922 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FKV
- Type
- protein
- Length
- 1,009 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q72KD3
- Ligands
- SO4, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 504 | — | Q72KD3 |
| B | — | protein | 505 | — | Q72KD3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FKV · Structure and function of aldehyde dehydrogenase from Thermus thermophilus: An enzyme… · 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 Q72KD3
- Elsewhere: RCSB PDB 6FKV · PDBe 6FKV · UniProt Q72KD3
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