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Asymmetric unit of cryoem structure of bacteriophage lambda capsid at 3.76 ångström

Analyse Asymmetric unit of cryoem structure of bacteriophage lambda capsid at 3.76… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VIK
Type
protein
Length
3,136 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major capsid protein; Capsid decoration protein
UniProt
P03713, P03712
Pockets
20 · best druggability 0.72

Structure

electron microscopy · 2 distinct chains · 15% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GMajor capsid proteinprotein33919% helix, 24% strandP03713
H, I, J, K, L, M, NCapsid decoration proteinprotein1095% helix, 32% strandP03712

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16820.720.7987empty
24520.690.8079empty
31140.690.9124empty
41210.680.9026empty
52570.630.8147empty

Interfaces

38 interfaces between chains.

  • A–B · 3242 Ų buried · 45 hydrogen bonds · protein-protein
  • D–E · 3155 Ų buried · 38 hydrogen bonds · protein-protein
  • C–D · 3086 Ų buried · 39 hydrogen bonds · protein-protein
  • A–F · 3071 Ų buried · 40 hydrogen bonds · protein-protein
  • E–F · 3064 Ų buried · 42 hydrogen bonds · protein-protein

Compared structures

  • 7VIK · Asymmetric unit of cryoEM structure of bacteriophage lambda capsid at 3.76 Angstrom · the same entry in another collection · chain A against A, TM-score 1.00

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