MolNFT v1 · #148222 · protein

Crystal structure ASF1-IP2_S

6F0F · Histone chaperone ASF1A: “Crystal structure ASF1-IP2_S”. X-ray diffraction. MolNFT v1 #148222 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6F0F
Type: protein
Length: 183 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone ASF1A; IP2_S
UniProt: Q9Y294

Structure

x-ray diffraction · 2 distinct chains · 16% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone chaperone ASF1A	protein	155	12% helix, 51% strand	Q9Y294
B	IP2_S	protein	28	39% helix, 11% strand	—

Interfaces

1 interface between chains.

A–B · 952 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

6F0F · Crystal structure ASF1-ip2_s · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y294 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9Y294
Elsewhere: RCSB PDB 6F0F · PDBe 6F0F · UniProt Q9Y294

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