MolNFT v1 · #18336 · protein

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

1PLJ · C-H-RAS P21 protein: “Crystallographic studies on P21H-RAS using synchrotron laue method: improvement of crystal quality and…”. X-ray diffraction, 2 ligands (CAG, MG), 4 pockets (best druggability 0.65). MolNFT v1 #18336 on…

PDB: 1PLJ
Type: protein
Length: 147 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: C-H-RAS P21 protein
UniProt: P01112
Ligands: CAG, MG
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	C-H-RAS P21 protein	protein	147	27% helix, 16% strand	P01112

Ligands and binding sites

CAG · Guanosine 5'-triphosphate P3-[1-(2-nitrophenyl)ethyl ester] · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

4 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	73	0.65	0.93	25	empty
2	127	0.50	0.80	18	empty
3	123	0.41	0.76	27	MG, CAG
4	80	0.40	0.78	14	empty

Compared structures

1PLJ · 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 1PLJ · PDBe 1PLJ · UniProt P01112

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