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Crystal structure of SPCIA1/ASF1 complexed with CAC2 peptide

Analyse Crystal structure of SPCIA1/ASF1 complexed with CAC2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z3F
Type
protein
Length
1,370 residues
Chains
19
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone chaperone CIA1; SPAC26H5.03 protein
UniProt
O74515, O13985
Pockets
17 · best druggability 0.79

Structure

x-ray diffraction · 6 distinct chains · 12% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, G, HHistone chaperone CIA1protein16012% helix, 49% strandO74515
I, J, M, N, O, PSPAC26H5.03 proteinprotein100% helix, 60% strandO13985
KSPAC26H5.03 proteinprotein70% helix, 43% strandO13985
LSPAC26H5.03 proteinprotein90% helix, 33% strandO13985
FHistone chaperone CIA1protein15914% helix, 48% strandO74515
Q, R, TSPAC26H5.03 proteinprotein50% helix, 0% strandO13985

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17080.790.8385empty
24960.710.8049empty
34040.700.8251empty
46090.660.7663empty
53620.630.7948empty

Interfaces

39 interfaces between chains.

  • E–G · 888 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 885 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 873 Ų buried · 6 hydrogen bonds · protein-protein
  • F–H · 870 Ų buried · 7 hydrogen bonds · protein-protein
  • D–H · 583 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 2Z3F · Crystal structure of spCia1/Asf1 complexed with Cac2 peptide · the same entry in another collection · chain D against D, TM-score 1.00

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