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Crystal structure of the drosophila kinesin family member KIN10/NOD in complex with divalent manganese and ADP

Analyse Crystal structure of the drosophila kinesin family member KIN10/NOD in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PXN
Type: protein
Length: 291 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein nod
UniProt: P18105
Ligands: ADP, MN
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein nod	protein	291	33% helix, 24% strand	P18105

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MN · Manganese (II) ion · metal · 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	109	0.46	0.79	21	empty

Compared structures

3PXN · Crystal structure of the Drosophila kinesin family member Kin10/NOD in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P18105 · AlphaFold monomer V2.0 prediction for kinesin-like protein nod (P18105) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P18105
Elsewhere: RCSB PDB 3PXN · PDBe 3PXN · UniProt P18105

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