MolNFT v1 · #181208 · protein

Apo structure of the histone chaperone ASF1A residues 1-155

7LNY: “Apo structure of the histone chaperone ASF1A residues 1-155”. X-ray diffraction. MolNFT v1 #181208 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LNY
Type: protein
Length: 1,078 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9Y294

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	—	protein	155	—	Q9Y294
C, E	—	protein	154	—	Q9Y294
F	—	protein	153	—	Q9Y294
G	—	protein	152	—	Q9Y294

Compared structures

7LNY · Apo structure of the Histone chaperone ASF1A residues 1-155 · the same entry in another collection · chain G against G, TM-score 1.00
Q9Y294 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294) · a predicted model of the same protein · chain G 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 7LNY · PDBe 7LNY · UniProt Q9Y294

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