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Crystal structure of the calponin-homology domain of RNG2 from schizosaccharomyces pombe

Analyse Crystal structure of the calponin-homology domain of RNG2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1P2X
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAS GTPase-activating-like protein
UniProt: O14188
Ligands: BR
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS GTPase-activating-like protein	protein	159	58% helix, 0% strand	O14188

Ligands and binding sites

BR · Bromide ion · ion · 11 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.31	0.74	16	BR

Compared structures

1P2X · Crystal structure of the calponin-homology domain of RNG2 from schizosaccharomyces pombe · the same entry in another collection · chain A against A, TM-score 1.00
O14188 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating-like protein RNG2 (O14188) · 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 O14188
Elsewhere: RCSB PDB 1P2X · PDBe 1P2X · UniProt O14188

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