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Crystal structure of the human retinitis pigmentosa protein 2 (RP2)

Analyse Crystal structure of the human retinitis pigmentosa protein 2 (RP2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BX6
Type
protein
Length
311 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
XRP2 protein
UniProt
O75695
Ligands
SO4
Pockets
3 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AXRP2 proteinprotein31125% helix, 33% strandO75695

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11510.480.7728empty
2930.390.7728empty
3510.260.7312empty

Compared structures

  • 2BX6 · Crystal Structure of the human Retinitis Pigmentosa protein 2 (RP2) · the same entry in another collection · chain A against A, TM-score 1.00
  • O75695 · AlphaFold monomer V2.0 prediction for protein XRP2 (O75695) · a predicted model of the same protein · chain A against A, TM-score 0.99

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