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Crystal structure analysis of a fluorescent form of H-RAS P21 in complex with R-caged GTP

Analyse Crystal structure analysis of a fluorescent form of H-RAS P21 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EVW
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase HRAS
UniProt: P01112
Ligands: CAG, XY2, MG
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	GTPase HRAS	protein	166	36% helix, 25% strand	P01112

Ligands and binding sites

CAG · Guanosine 5'-triphosphate P3-[1-(2-nitrophenyl)ethyl ester] · ligand · chains X
XY2 · N,N'-dimethyl-N-(acetyl)-N'-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)ethylenediamine · ligand · chains X
MG · Magnesium ion · metal · chains X

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	186	0.48	0.76	30	MG, CAG

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2EVW · Crystal structure analysis of a fluorescent form of H-Ras p21 in complex with R-caged GTP · the same entry in another collection · chain X against X, 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 2EVW · PDBe 2EVW · UniProt P01112

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