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Double-heterohexameric rings of full-length RVB1(ATP)/RVB2(APO)

Analyse Double-heterohexameric rings of full-length RVB1(ATP)/RVB2(APO) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WVY
Type: protein
Length: 835 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ruvb-like 1; Ruvb-like 2
UniProt: G0RYI5, G0RYC2
Ligands: ATP
Pockets: 15 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ruvb-like 1	protein	427	39% helix, 22% strand	G0RYI5
B	Ruvb-like 2	protein	408	38% helix, 23% strand	G0RYC2

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A

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

Pockets

15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	757	0.84	0.87	81	ATP
2	677	0.81	0.86	70	empty
3	62	0.60	0.90	12	empty
4	241	0.57	0.78	28	empty
5	250	0.55	0.77	28	empty

Interfaces

1 interface between chains.

A–B · 2432 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4WVY · Double-heterohexameric rings of full-length Rvb1(ATP)/Rvb2(apo) · the same entry in another collection · chain A against A, TM-score 1.00

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 G0RYI5
Every structure of UniProt G0RYC2
Elsewhere: RCSB PDB 4WVY · PDBe 4WVY · UniProt G0RYI5 · UniProt G0RYC2

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