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Cryo-EM structure of a bcsb pentamer in the context of an assembled bcs macrocomplex

Analyse Cryo-EM structure of a bcsb pentamer in the context of an assembled bcs… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YG8
Type
protein
Length
3,132 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bacterial cellulose secretion regulator bcsb
UniProt
A0A061KLG7
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 4 distinct chains · 15% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABacterial cellulose secretion regulator bcsbprotein64315% helix, 38% strandA0A061KLG7
B, CBacterial cellulose secretion regulator bcsbprotein63716% helix, 37% strandA0A061KLG7
DBacterial cellulose secretion regulator bcsbprotein63914% helix, 35% strandA0A061KLG7
EBacterial cellulose secretion regulator bcsbprotein57614% helix, 35% strandA0A061KLG7

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16450.800.8570empty
25850.780.8448empty
36180.760.8364empty
47030.760.81116empty
56740.750.8153empty

Interfaces

7 interfaces between chains.

  • B–D · 3491 Ų buried · 59 hydrogen bonds · protein-protein
  • A–C · 3471 Ų buried · 55 hydrogen bonds · protein-protein
  • A–B · 3449 Ų buried · 42 hydrogen bonds · protein-protein
  • C–E · 3419 Ų buried · 54 hydrogen bonds · protein-protein
  • A–E · 26 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 6YG8 · Cryo-EM structure of a BcsB pentamer in the context of an assembled Bcs macrocomplex · the same entry in another collection · chain E against E, TM-score 1.00

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