MolNFT v1 · #149351 · protein

Crystal structure of full-length human lysyl hydroxylase LH3 - cocrystal with FE2+, MN2+, udp-gal - structure from long-wavelength S-sad

6FXY: “Crystal structure of full-length human lysyl hydroxylase LH3 - cocrystal with FE2+, MN2+, udp-gal - structure…”. X-ray diffraction, 5 ligands (AKG, UDP, NAG). MolNFT v1 #149351 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6FXY
Type: protein
Length: 700 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O60568
Ligands: AKG, UDP, NAG, FE2, MN

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	700	—	O60568

Ligands and binding sites

AKG · 2-oxoglutaric acid · ligand · chains A
UDP · Uridine-5'-diphosphate · 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

6FXY · Crystal Structure of full-length Human Lysyl Hydroxylase LH3 - Cocrystal with Fe2+, Mn2+… · 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 6FXY · PDBe 6FXY · UniProt O60568

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