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The active site of the molybdenum cofactor biosenthetic protein domain CNX1G

Analyse The active site of the molybdenum cofactor biosenthetic protein domain CNX1G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1O8Q
Type
protein
Length
1,272 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Molybdopterin biosynthesis CNX1 protein
UniProt
Q39054
Pockets
7 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, HMolybdopterin biosynthesis CNX1 proteinprotein15947% helix, 22% strandQ39054

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110940.820.83143empty
210740.820.83136empty
31340.650.8842empty
41230.650.8841empty
52170.530.7742empty

Interfaces

10 interfaces between chains.

  • A–C · 835 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 834 Ų buried · 7 hydrogen bonds · protein-protein
  • D–F · 833 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 829 Ų buried · 7 hydrogen bonds · protein-protein
  • E–F · 829 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1O8Q · The active site of the molybdenum cofactor biosenthetic protein domain Cnx1G · the same entry in another collection · chain H against H, TM-score 1.00
  • Q39054 · AlphaFold monomer V2.0 prediction for molybdopterin biosynthesis protein CNX1 (Q39054) · a predicted model of the same protein · chain B against A, TM-score 0.99

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