GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the FN4-FN6 domains of human ptprd

Analyse Crystal structure of the FN4-FN6 domains of human ptprd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6X3A
Type
protein
Length
306 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Receptor-type tyrosine-protein phosphatase delta
EC
3.1.3.48
UniProt
P23468

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReceptor-type tyrosine-protein phosphatase delta (EC 3.1.3.48)protein3063% helix, 52% strandP23468

Ligands and binding sites

  • GOL · Glycerol · additive · chains A

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

Compared structures

  • 6X3A · Crystal structure of the FN4-FN6 domains of human PTPRD · the same entry in another collection · chain A against A, TM-score 1.00
  • P23468 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase delta… · a predicted model of the same protein · chain A against A, TM-score 0.70

Analyse

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