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Crystal structure of a VPS33-VPS16 complex from chaetomium thermophilum

Analyse Crystal structure of a VPS33-VPS16 complex from chaetomium thermophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5BV1
Type
protein
Length
1,797 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
VPS33; Putative vacuolar protein sorting-associated protein
UniProt
G0SCM5, G0S6M7
Ligands
MLT
Pockets
20 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 53% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVPS33protein60149% helix, 15% strandG0SCM5
B, DPutative vacuolar protein sorting-associated proteinprotein29768% helix, 0% strandG0S6M7
CVPS33protein60250% helix, 15% strandG0SCM5

Ligands and binding sites

  • MLT · D-malate · ligand · 2 copies · chains B, D

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

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19710.800.82105MLT
26830.780.8371empty
3530.720.9919empty
43420.650.8041empty
52890.640.8035empty

Interfaces

4 interfaces between chains.

  • A–B · 2349 Ų buried · 19 hydrogen bonds · protein-protein
  • C–D · 2315 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 131 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 56 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5BV1 · Crystal Structure of a Vps33-Vps16 Complex from Chaetomium thermophilum · the same entry in another collection · chain A against A, TM-score 1.00

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