MolNFT v1 · #149337 · protein
Crystal structure of full-length human lysyl hydroxylase LH3
6FXK: “Crystal structure of full-length human lysyl hydroxylase LH3”. X-ray diffraction, 3 ligands (AKG, NAG, FE2). MolNFT v1 #149337 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6FXK
- Type
- protein
- Length
- 670 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60568
- Ligands
- AKG, NAG, FE2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 670 | — | O60568 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- FE2 · Fe (II) ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- O60568 · AlphaFold monomer V2.0 prediction for multifunctional procollagen lysine hydroxylase and… · 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 O60568
- Elsewhere: RCSB PDB 6FXK · PDBe 6FXK · UniProt O60568
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