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Crystal structure of SFH5

Analyse Crystal structure of SFH5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6W32
Type
protein
Length
852 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphatidylinositol transfer protein SFH5
UniProt
A6ZQI5
Ligands
HEM
Pockets
15 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BPhosphatidylinositol transfer protein SFH5protein28849% helix, 11% strandA6ZQI5
APhosphatidylinositol transfer protein SFH5protein27842% helix, 12% strandA6ZQI5
CPhosphatidylinositol transfer protein SFH5protein28639% helix, 8% strandA6ZQI5

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains B, A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14060.850.9248HEM
23870.840.9253HEM
34650.820.8955HEM
41020.760.9627empty
5860.730.9626empty

Interfaces

2 interfaces between chains.

  • B–A · 942 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 475 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 6W32 · Crystal structure of Sfh5 · the same entry in another collection · chain B against B, TM-score 1.00
  • A6ZQI5 · AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein SFH5 (A6ZQI5) · a predicted model of the same protein · chain B against A, TM-score 0.97

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