GL1X · GenesisL1 explorer

MolNFT v1 · #56047 · protein

Crystal structure of SPCIA1/ASF1 complex with HIP1

2Z34 · Histone chaperone CIA1: “Crystal structure of SPCIA1/ASF1 complex with HIP1”. X-ray diffraction, 3 pockets (best druggability 0.75). MolNFT v1 #56047 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
2Z34
Type
protein
Length
347 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone chaperone CIA1; Protein HIR1
UniProt
O74515, P87314
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone chaperone CIA1protein1556% helix, 50% strandO74515
BHistone chaperone CIA1protein1497% helix, 52% strandO74515
CProtein HIR1protein210% helix, 48% strandP87314
DProtein HIR1protein220% helix, 45% strandP87314

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13810.750.8657empty
22170.570.8038empty
3800.360.7616empty

Interfaces

6 interfaces between chains.

  • A–B · 844 Ų buried · 5 hydrogen bonds · protein-protein
  • B–D · 748 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 733 Ų buried · 16 hydrogen bonds · protein-protein
  • A–D · 253 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 249 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 2Z34 · Crystal structure of SpCia1/Asf1 complex with Hip1 · the same entry in another collection · chain D against D, TM-score 1.00
  • O74515 · AlphaFold monomer V2.0 prediction for histone chaperone CIA1 (O74515) · a predicted model of the same protein · chain B against A, TM-score 0.93
  • P87314 · AlphaFold monomer V2.0 prediction for protein HIR1 (P87314) · a predicted model of the same protein · chain D against A, TM-score 0.43

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