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Structure of MYO2-gtd in complex with SMY1

Analyse Structure of MYO2-gtd in complex with SMY1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IXQ
Type: protein
Length: 406 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myosin-2; Kinesin-related protein SMY1
UniProt: P19524, P32364
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 67% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myosin-2	protein	391	69% helix, 2% strand	P19524
B	Kinesin-related protein SMY1	protein	15	0% helix, 13% strand	P32364

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	108	0.48	0.80	23	empty

Interfaces

1 interface between chains.

A–B · 897 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6IXQ · Structure of Myo2-GTD in complex with Smy1 · the same entry in another collection · chain A against A, TM-score 1.00
P19524 · AlphaFold monomer V2.0 prediction for myosin-2 (P19524) · a predicted model of the same protein · chain A against A, TM-score 0.98
P32364 · AlphaFold monomer V2.0 prediction for kinesin-related protein SMY1 (P32364) · a predicted model of the same protein · chain B against A, TM-score 0.20

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 P19524
Every structure of UniProt P32364
Elsewhere: RCSB PDB 6IXQ · PDBe 6IXQ · UniProt P19524 · UniProt P32364

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