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Two surfaces on RTT106 mediate histone binding and chaperone activity

Analyse Two surfaces on RTT106 mediate histone binding and chaperone activity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TO1
Type: protein
Length: 423 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone RTT106
UniProt: P40161
Pockets: 3 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone chaperone RTT106	protein	212	19% helix, 49% strand	P40161
B	Histone chaperone RTT106	protein	211	20% helix, 49% strand	P40161

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	193	0.44	0.73	24	empty
2	63	0.29	0.74	17	empty
3	52	0.25	0.73	13	empty

Interfaces

1 interface between chains.

A–B · 103 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3TO1 · Two surfaces on Rtt106 mediate histone binding and chaperone activity · the same entry in another collection · chain A against A, TM-score 1.00
P40161 · AlphaFold monomer V2.0 prediction for histone chaperone RTT106 (P40161) · 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 P40161
Elsewhere: RCSB PDB 3TO1 · PDBe 3TO1 · UniProt P40161

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