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Crystal structure of the plant rho protein ROP5

Analyse Crystal structure of the plant rho protein ROP5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BWD
Type: protein
Length: 156 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rac-like GTP-binding protein ARAC6
UniProt: Q9SBJ6
Ligands: GDP, MG

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	Rac-like GTP-binding protein ARAC6	protein	156	42% helix, 17% strand	Q9SBJ6

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains D
MG · Magnesium ion · metal · chains D

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

Compared structures

3BWD · Crystal structure of the plant Rho protein ROP5 · the same entry in another collection · chain D against D, TM-score 1.00
Q9SBJ6 · AlphaFold monomer V2.0 prediction for rac-like GTP-binding protein ARAC6 (Q9SBJ6) · a predicted model of the same protein · chain D against A, TM-score 0.97

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 Q9SBJ6
Elsewhere: RCSB PDB 3BWD · PDBe 3BWD · UniProt Q9SBJ6

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