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Crystal structure of maze-mazf (form-I) from deinococcus radiodurans

Analyse Crystal structure of maze-mazf (form-I) from deinococcus radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7D2Q
Type
protein
Length
475 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endoribonuclease mazf; ABRB/MAZE/SPOVT family DNA-binding domain-containing protein
EC
3.1.27.-
UniProt
A0A6G9BVQ8, A0A6G9BVE7
Pockets
4 · best druggability 0.56

Structure

x-ray diffraction · 5 distinct chains · 25% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndoribonuclease mazf (EC 3.1.27.-)protein10024% helix, 31% strandA0A6G9BVQ8
CEndoribonuclease mazf (EC 3.1.27.-)protein10327% helix, 33% strandA0A6G9BVQ8
D, FABRB/MAZE/SPOVT family DNA-binding domain-containing proteinprotein3020% helix, 0% strandA0A6G9BVE7
EEndoribonuclease mazf (EC 3.1.27.-)protein10225% helix, 32% strandA0A6G9BVQ8
GEndoribonuclease mazf (EC 3.1.27.-)protein11025% helix, 32% strandA0A6G9BVQ8

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12370.560.7842empty
23020.540.7533empty
3870.330.7422empty
4700.330.7519empty

Interfaces

11 interfaces between chains.

  • E–F · 1281 Ų buried · 23 hydrogen bonds · protein-protein
  • C–D · 1213 Ų buried · 19 hydrogen bonds · protein-protein
  • A–E · 886 Ų buried · 11 hydrogen bonds · protein-protein
  • C–G · 874 Ų buried · 10 hydrogen bonds · protein-protein
  • A–F · 629 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 7D2Q · Crystal structure of MazE-MazF (Form-I) from Deinococcus radiodurans · the same entry in another collection · chain A against A, TM-score 1.00

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