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Osm-3 kinesin motor domain complexed with MG.ADP

Analyse Osm-3 kinesin motor domain complexed with MG.ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A3Z
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Osmotic avoidance abnormal protein 3
UniProt: P46873
Ligands: ADP, MG
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Osmotic avoidance abnormal protein 3	protein	307	32% helix, 31% strand	P46873

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	119	0.59	0.85	22	empty
2	116	0.44	0.77	23	empty

Compared structures

7A3Z · OSM-3 kinesin motor domain complexed with Mg.ADP · the same entry in another collection · chain A against A, TM-score 1.00
P46873 · AlphaFold monomer V2.0 prediction for osmotic avoidance abnormal protein 3 (P46873) · 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 P46873
Elsewhere: RCSB PDB 7A3Z · PDBe 7A3Z · UniProt P46873

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