MolNFT v1 · #33230 · protein

Crystal structure analysis of a fluorescent form of H-RAS P21 in complex with GDP

2CE2 · GTPase HRAS: “Crystal structure analysis of a fluorescent form of H-RAS P21 in complex with GDP”. X-ray diffraction, 3 ligands (GDP, XY2, MG), 2 pockets (best druggability 0.43). MolNFT v1 #33230 on GenesisL1: 3D structure, binding…

PDB: 2CE2
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: GDP, XY2, MG
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	GTPase HRAS	protein	166	37% helix, 26% strand	P01112

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	119	0.43	0.77	30	MG, GDP
2	82	0.39	0.78	17	empty

Modifications

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

Compared structures

2CE2 · Crystal structure analysis of a fluorescent form of H-RAS P21 in complex with GDP · 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 2CE2 · PDBe 2CE2 · UniProt P01112

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