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Crystal structure of the native CHAPERONE:SUBUNIT:SUBUNIT CAF1M:CAF1:CAF1 complex

Analyse Crystal structure of the native CHAPERONE:SUBUNIT:SUBUNIT CAF1M:CAF1:CAF1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Z9S
Type
protein
Length
473 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperone protein CAF1M; F1 capsule antigen
UniProt
P26926, P26948
Pockets
4 · best druggability 0.61

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein CAF1Mprotein1963% helix, 57% strandP26926
BF1 capsule antigenprotein1492% helix, 52% strandP26948
CF1 capsule antigenprotein1282% helix, 49% strandP26948

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11810.610.8434empty
22810.530.7546empty
3600.420.8217empty
41470.400.7329empty

Interfaces

3 interfaces between chains.

  • A–B · 1787 Ų buried · 46 hydrogen bonds · protein-protein
  • B–C · 1141 Ų buried · 32 hydrogen bonds · protein-protein
  • A–C · 275 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1Z9S · Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P26926 · AlphaFold monomer V2.0 prediction for chaperone protein CAF1M (P26926) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • P26948 · AlphaFold monomer V2.0 prediction for F1 capsule antigen (P26948) · a predicted model of the same protein · chain C against A, TM-score 0.96

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