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Crystallographic studies on P21H-RAS using synchrotron laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time points

Analyse Crystallographic studies on P21H-RAS using synchrotron laue method: improvement… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PLL
Type: protein
Length: 154 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-H-RAS P21 protein
UniProt: P01112
Ligands: GDP
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-H-RAS P21 protein	protein	154	22% helix, 9% strand	P01112

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A

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

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	282	0.74	0.87	57	empty
2	72	0.71	0.96	22	empty
3	64	0.42	0.81	13	GDP

Compared structures

1PLL · Crystallographic studies on P21H-RAS using synchrotron laue method: improvement of… · the same entry in another collection · chain A against A, TM-score 1.00

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 P01112
Elsewhere: RCSB PDB 1PLL · PDBe 1PLL · UniProt P01112

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