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Crystal structure of the C-terminal part of FUN30 ATPase domain

Analyse Crystal structure of the C-terminal part of FUN30 ATPase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GN1
Type
protein
Length
1,240 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent helicase FUN30
EC
3.6.4.12
UniProt
P31380
Pockets
19 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 55% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATP-dependent helicase FUN30 (EC 3.6.4.12)protein30954% helix, 11% strandP31380
BATP-dependent helicase FUN30 (EC 3.6.4.12)protein30955% helix, 11% strandP31380
CATP-dependent helicase FUN30 (EC 3.6.4.12)protein31054% helix, 11% strandP31380
DATP-dependent helicase FUN30 (EC 3.6.4.12)protein31255% helix, 11% strandP31380

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110150.760.7984empty
211010.720.7680empty
32550.570.7826empty
42980.550.7630empty
52610.510.7430empty

Interfaces

6 interfaces between chains.

  • A–D · 434 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 399 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 217 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 213 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 206 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5GN1 · Crystal structure of the C-terminal part of Fun30 ATPase domain · the same entry in another collection · chain D against D, TM-score 1.00
  • P31380 · AlphaFold monomer V2.0 prediction for ATP-dependent helicase FUN30 (P31380) · a predicted model of the same protein · chain C against A, TM-score 0.92

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