GL1X · GenesisL1 explorer

Research workbench

X-ray structure of the phosphatase PAPP5 from arabidopsis thaliana

Analyse X-ray structure of the phosphatase PAPP5 from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OBE
Type
protein
Length
955 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Isoform 2 of SERINE/THREONINE-protein phosphatase 5
EC
3.1.3.16
UniProt
Q84XU2
Ligands
MN, CL
Pockets
6 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIsoform 2 of SERINE/THREONINE-protein phosphatase 5 (EC 3.1.3.16)protein48047% helix, 13% strandQ84XU2
BIsoform 2 of SERINE/THREONINE-protein phosphatase 5 (EC 3.1.3.16)protein47548% helix, 12% strandQ84XU2

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 4 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110370.820.83107empty
21870.750.9124empty
32400.680.8421empty
42080.650.8450CL
5940.580.8620empty

Interfaces

1 interface between chains.

  • A–B · 755 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 7OBE · X-ray structure of the phosphatase PAPP5 from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
  • Q84XU2 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 5 (Q84XU2) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

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