Research workbench

Crystal structure of the C2-gap fragment of syngap

Analyse Crystal structure of the C2-gap fragment of syngap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BXJ
Type: protein
Length: 706 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAS GTPase-activating protein syngap
UniProt: Q9QUH6
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 63% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS GTPase-activating protein syngap	protein	348	64% helix, 6% strand	Q9QUH6
B	RAS GTPase-activating protein syngap	protein	358	63% helix, 7% strand	Q9QUH6

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	771	0.73	0.78	80	empty
2	1034	0.72	0.76	95	empty
3	104	0.34	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 1684 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

3BXJ · Crystal Structure of the C2-GAP Fragment of synGAP · the same entry in another collection · chain A against A, TM-score 1.00
Q9QUH6 · AlphaFold monomer V2.0 prediction for RAS/RAP GTPase-activating protein syngap (Q9QUH6) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q9QUH6
Elsewhere: RCSB PDB 3BXJ · PDBe 3BXJ · UniProt Q9QUH6

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