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Structure of SPAC806.04C protein from fission yeast covalently bound to BEF3

Analyse Structure of SPAC806.04C protein from fission yeast covalently bound to BEF3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7U1X
Type
protein
Length
873 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Damage-control phosphatase SPAC806.04C
EC
3.1.3.-
UniProt
Q9UT55
Ligands
ZN, PO4
Pockets
6 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADamage-control phosphatase SPAC806.04C (EC 3.1.3.-)protein43956% helix, 10% strandQ9UT55
BDamage-control phosphatase SPAC806.04C (EC 3.1.3.-)protein43455% helix, 11% strandQ9UT55

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · chains 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18910.790.8197empty
2890.490.8114empty
31500.450.7623empty
4850.420.7825empty
5570.370.7917empty

Interfaces

1 interface between chains.

  • A–B · 945 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

  • 7U1X · Structure of SPAC806.04c protein from fission yeast covalently bound to BeF3 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UT55 · AlphaFold monomer V2.0 prediction for damage-control phosphatase SPAC806.04C (Q9UT55) · a predicted model of the same protein · chain B against A, TM-score 0.94

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