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The capsid of myoviridae phage XM1

Analyse The capsid of myoviridae phage XM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KMX
Type
protein
Length
3,178 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Minor capsid protein; Major capsid protein
Pockets
20 · best druggability 0.70

Structure

electron microscopy · 2 distinct chains · 17% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
a, b, c, d, e, f, gMinor capsid proteinprotein1600% helix, 42% strand—
A, B, C, D, E, F, GMajor capsid proteinprotein29426% helix, 32% strand—

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14190.700.8141empty
27340.700.7774empty
35990.690.7872empty
45820.670.7753empty
53150.660.8141empty

Interfaces

29 interfaces between chains.

  • A–B · 2464 Ų buried · 35 hydrogen bonds · protein-protein
  • E–F · 2439 Ų buried · 31 hydrogen bonds · protein-protein
  • D–E · 2429 Ų buried · 27 hydrogen bonds · protein-protein
  • C–D · 2422 Ų buried · 38 hydrogen bonds · protein-protein
  • A–F · 2410 Ų buried · 41 hydrogen bonds · protein-protein

Compared structures

  • 7KMX · The capsid of Myoviridae Phage XM1 · the same entry in another collection · chain a against a, TM-score 1.00

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