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Crystal structure of the PRP38-MFAP1 complex of chaetomium thermophilum

Analyse Crystal structure of the PRP38-MFAP1 complex of chaetomium thermophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5F5T
Type
protein
Length
537 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative uncharacterized protein
UniProt
G0S1D3, G0SHD7
Pockets
3 · best druggability 0.79

Structure

x-ray diffraction · 4 distinct chains · 62% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative uncharacterized proteinprotein21557% helix, 9% strandG0S1D3
BPutative uncharacterized proteinprotein21458% helix, 9% strandG0S1D3
CPutative uncharacterized proteinprotein6481% helix, 0% strandG0SHD7
DPutative uncharacterized proteinprotein4480% helix, 0% strandG0SHD7

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110980.790.8189empty
22500.590.7934empty
32230.590.8034empty

Interfaces

6 interfaces between chains.

  • A–C · 1140 Ų buried · 20 hydrogen bonds · protein-protein
  • B–D · 1129 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 446 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 381 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 224 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 5F5T · Crystal structure of the Prp38-MFAP1 complex of Chaetomium thermophilum · the same entry in another collection · chain A against A, TM-score 1.00

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