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Crystal structure of the gap domain of MGCRACGAP(S387A)

Analyse Crystal structure of the gap domain of MGCRACGAP(S387A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WPQ
Type: protein
Length: 398 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rac GTPase-activating protein 1
UniProt: Q9H0H5
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rac GTPase-activating protein 1	protein	200	62% helix, 0% strand	Q9H0H5
B	Rac GTPase-activating protein 1	protein	198	63% helix, 0% strand	Q9H0H5

Pockets

2 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	668	0.75	0.81	77	empty
2	64	0.27	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 781 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3WPQ · crystal structure of the GAP domain of MgcRacGAP(S387A) · the same entry in another collection · chain A against A, TM-score 1.00
Q9H0H5 · AlphaFold monomer V2.0 prediction for rac GTPase-activating protein 1 (Q9H0H5) · 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 Q9H0H5
Elsewhere: RCSB PDB 3WPQ · PDBe 3WPQ · UniProt Q9H0H5

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