Research workbench

Truncated human R2TP complex, structure 3 (ADP-filled)

Analyse Truncated human R2TP complex, structure 3 (ADP-filled) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QI8
Type: protein
Length: 1,907 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9Y265, Q9Y230
Ligands: ADP

Structure

electron microscopy · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	317	—	Q9Y265
B	—	protein	310	—	Q9Y265
C	—	protein	316	—	Q9Y265
D	—	protein	296	—	Q9Y230
E	—	protein	335	—	Q9Y230
F	—	protein	333	—	Q9Y230

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F

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

Compared structures

6QI8 · Truncated human R2TP complex, structure 3 (ADP-filled) · the same entry in another collection · chain F against F, TM-score 1.00
Q9Y265 · AlphaFold monomer V2.0 prediction for ruvb-like 1 (Q9Y265) · a predicted model of the same protein · chain C against A, TM-score 0.91

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 Q9Y265
Every structure of UniProt Q9Y230
Elsewhere: RCSB PDB 6QI8 · PDBe 6QI8 · UniProt Q9Y265 · UniProt Q9Y230

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