GL1X · GenesisL1 explorer

Research workbench

GAPDH purified from the supernatant of HEK293F cells: crystal form 4 of 4

Analyse GAPDH purified from the supernatant of HEK293F cells: crystal form 4 of 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YNH
Type
protein
Length
1,336 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P04406

Structure

x-ray diffraction · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
B, D, F, G—protein334—P04406

Ligands and binding sites

  • XPE · 3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diol · additive · 4 copies · chains B, D, F, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 6YNH · GAPDH purified from the supernatant of HEK293F cells: crystal form 4 of 4 · the same entry in another collection · chain G against G, TM-score 1.00
  • P04406 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P04406) · a predicted model of the same protein · chain G against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.