Research workbench

Crystal structure of rev-erb beta

Analyse Crystal structure of rev-erb beta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2V7C
Type: protein
Length: 340 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orphan nuclear receptor NR1D2
UniProt: Q14995
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 67% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orphan nuclear receptor NR1D2	protein	165	63% helix, 4% strand	Q14995
B	Orphan nuclear receptor NR1D2	protein	175	71% helix, 5% strand	Q14995

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	420	0.70	0.81	50	empty
2	192	0.66	0.85	25	empty
3	76	0.38	0.77	14	empty
4	100	0.35	0.73	24	empty
5	70	0.33	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1031 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

2V7C · Crystal Structure of Rev-Erb beta · the same entry in another collection · chain A against A, TM-score 1.00
Q14995 · AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 1 group D member 2… · a predicted model of the same protein · chain A 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 Q14995
Elsewhere: RCSB PDB 2V7C · PDBe 2V7C · UniProt Q14995

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.