MolNFT v1 · #161547 · protein
Time resolved structural analysis of the full turnover of an enzyme - 376 ms
6QHT: “Time resolved structural analysis of the full turnover of an enzyme - 376 ms”. X-ray diffraction, 1 ligand (FAH). MolNFT v1 #161547 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6QHT
- Type
- protein
- Length
- 597 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6NAM1
- Ligands
- FAH
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 299 | — | Q6NAM1 |
| B | — | protein | 298 | — | Q6NAM1 |
Ligands and binding sites
- FAH · fluoroacetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6QHT · Time resolved structural analysis of the full turnover of an enzyme - 376 ms · the same entry in another collection · chain A against A, TM-score 1.00
- Q6NAM1 · AlphaFold monomer V2.0 prediction for fluoroacetate dehalogenase (Q6NAM1) · a predicted model of the same protein · chain B 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 Q6NAM1
- Elsewhere: RCSB PDB 6QHT · PDBe 6QHT · UniProt Q6NAM1
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