MolNFT v1 · #32525 · protein

Structure of the regulator of G-protein signaling 16

2BT2: “Structure of the regulator of G-protein signaling 16”. X-ray diffraction, 3 pockets (best druggability 0.64). MolNFT v1 #32525 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2BT2
Type: protein
Length: 711 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulator of G-protein signaling 16
UniProt: O15492
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 5 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Regulator of G-protein signaling 16	protein	143	76% helix, 0% strand	O15492
B	Regulator of G-protein signaling 16	protein	142	71% helix, 0% strand	O15492
C	Regulator of G-protein signaling 16	protein	142	77% helix, 0% strand	O15492
D	Regulator of G-protein signaling 16	protein	141	74% helix, 0% strand	O15492
E	Regulator of G-protein signaling 16	protein	143	74% helix, 0% strand	O15492

Pockets

3 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	485	0.64	0.77	60	empty
2	187	0.54	0.79	29	empty
3	64	0.31	0.75	9	empty

Interfaces

4 interfaces between chains.

A–B · 504 Å² buried · 5 hydrogen bonds · protein-protein
D–E · 463 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 363 Å² buried · 2 hydrogen bonds · protein-protein
A–E · 347 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2BT2 · Structure of the regulator of G-protein signaling 16 · the same entry in another collection · chain E against E, TM-score 1.00
O15492 · AlphaFold monomer V2.0 prediction for regulator of G-protein signaling 16 (O15492) · 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 O15492
Elsewhere: RCSB PDB 2BT2 · PDBe 2BT2 · UniProt O15492

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