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HMIRO1 C-domain GDP-pi complex P3121 crystal form

Analyse HMIRO1 C-domain GDP-pi complex P3121 crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KSO
Type: protein
Length: 166 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitochondrial rho GTPase 1
EC: 3.6.5.-
UniProt: Q8IXI2
Ligands: GDP, PO4
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitochondrial rho GTPase 1 (EC 3.6.5.-)	protein	166	29% helix, 24% strand	Q8IXI2

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
PO4 · Phosphate ion · ion · chains A

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	84	0.39	0.77	22	GDP, PO4

Compared structures

5KSO · hMiro1 C-domain GDP-Pi Complex P3121 Crystal Form · the same entry in another collection · chain A against A, TM-score 1.00
Q8IXI2 · AlphaFold monomer V2.0 prediction for mitochondrial rho GTPase 1 (Q8IXI2) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q8IXI2
Elsewhere: RCSB PDB 5KSO · PDBe 5KSO · UniProt Q8IXI2

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