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Structure of the human beta-myosin S2 fragment

Analyse Structure of the human beta-myosin S2 fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FXO
Type
protein
Length
508 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myosin heavy chain, cardiac muscle beta isoform
UniProt
P12883
Pockets
4 · best druggability 0.41

Structure

x-ray diffraction · 4 distinct chains · 95% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMyosin heavy chain, cardiac muscle beta isoformprotein12995% helix, 0% strandP12883
BMyosin heavy chain, cardiac muscle beta isoformprotein12593% helix, 0% strandP12883
CMyosin heavy chain, cardiac muscle beta isoformprotein12796% helix, 0% strandP12883
DMyosin heavy chain, cardiac muscle beta isoformprotein12795% helix, 0% strandP12883

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11430.410.7420empty
21260.360.7218empty
31040.350.7418empty
41050.340.7323empty

Interfaces

5 interfaces between chains.

  • A–B · 3549 Ų buried · 23 hydrogen bonds · protein-protein
  • C–D · 3539 Ų buried · 17 hydrogen bonds · protein-protein
  • B–D · 398 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 312 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 78 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 2FXO · Structure of the human beta-myosin S2 fragment · the same entry in another collection · chain D against D, TM-score 1.00
  • P12883 · AlphaFold monomer V2.0 prediction for myosin-7 (P12883) · a predicted model of the same protein · chain D against A, TM-score 0.85

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