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RAS-GTPase-activating domain of human P120GAP

Analyse RAS-GTPase-activating domain of human P120GAP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WER
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P120GAP
UniProt: P20936
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P120GAP	protein	324	72% helix, 0% strand	P20936

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.52	0.83	22	empty
2	55	0.35	0.78	14	empty
3	67	0.29	0.73	13	empty

Compared structures

1WER · RAS-GTPase-activating domain of human P120GAP · the same entry in another collection · chain A against A, TM-score 1.00
P20936 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating protein 1 (P20936) · 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 P20936
Elsewhere: RCSB PDB 1WER · PDBe 1WER · UniProt P20936

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