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RTT106P

Analyse RTT106P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GYP
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone RTT106
UniProt: P40161
Ligands: CL

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone chaperone RTT106	protein	225	20% helix, 47% strand	P40161

Ligands and binding sites

CL · Chloride ion · ion · chains A
BME · Beta-mercaptoethanol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

3GYP · Rtt106p · 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 0.94

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 3GYP · PDBe 3GYP · UniProt P40161

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