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Crystal structure analysis of a full-length mcm homolog from methanopyrus kandleri

Analyse Crystal structure analysis of a full-length mcm homolog from methanopyrus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3F8T
Type
protein
Length
459 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Predicted ATPase involved in replication control, CDC46/MCM family
UniProt
Q8TWB5
Pockets
7 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APredicted ATPase involved in replication control, CDC46/MCM familyprotein45946% helix, 21% strandQ8TWB5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.520.8512empty
21780.430.7420empty
3790.420.8015empty
4610.370.7914empty
5520.330.7812empty

Compared structures

  • 3F8T · Crystal structure analysis of a full-length MCM homolog from Methanopyrus kandleri · the same entry in another collection · chain A against A, TM-score 1.00

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