MolNFT v1 · #164956 · protein
Crystal structure of full-length human lysyl hydroxylase LH3 - VAL80LYS mutant - cocrystal with FE2+, MN2+
6TEU: “Crystal structure of full-length human lysyl hydroxylase LH3 - VAL80LYS mutant - cocrystal with FE2+, MN2+”. X-ray diffraction, 4 ligands (AKG, NAG, FE2). MolNFT v1 #164956 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6TEU
- Type
- protein
- Length
- 691 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60568
- Ligands
- AKG, NAG, FE2, MN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 691 | — | 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 · 2 copies · chains A
- MN · Manganese (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
- 6TEU · Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Val80Lys mutant… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.98
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 6TEU · PDBe 6TEU · UniProt O60568
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