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Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions

Analyse Close packing of an oligomeric eye lens beta-crystallin induces loss of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BLB
Type
protein
Length
736 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta B2-crystallin
UniProt
P02522
Pockets
3 · best druggability 0.27

Structure

x-ray diffraction · 4 distinct chains · 5% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta B2-crystallinprotein1854% helix, 29% strandP02522
BBeta B2-crystallinprotein1816% helix, 31% strandP02522
CBeta B2-crystallinprotein1876% helix, 34% strandP02522
DBeta B2-crystallinprotein1834% helix, 39% strandP02522

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1580.270.7413empty
2600.260.7215empty
3530.240.7215empty

Interfaces

3 interfaces between chains.

  • C–D · 2137 Ų buried · 34 hydrogen bonds · protein-protein
  • A–B · 2086 Ų buried · 29 hydrogen bonds · protein-protein
  • A–D · 90 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1BLB · Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and… · the same entry in another collection · chain D against D, TM-score 1.00
  • P02522 · AlphaFold monomer V2.0 prediction for beta-crystallin B2 (P02522) · a predicted model of the same protein · chain C against A, TM-score 0.48

Analyse

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