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Human alphab crystallin acd R120G

Analyse Human alphab crystallin acd R120G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y1Z
Type
protein
Length
172 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-crystallin B chain
UniProt
P02511

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 59% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-crystallin B chainprotein857% helix, 56% strandP02511
BAlpha-crystallin B chainprotein877% helix, 61% strandP02511

Ligands and binding sites

  • MRD · (4R)-2-methylpentane-2,4-diol · additive · 3 copies · chains A, B
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 1031 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 2Y1Z · Human alphaB Crystallin ACD R120G · the same entry in another collection · chain A against A, TM-score 1.00
  • P02511 · AlphaFold monomer V2.0 prediction for alpha-crystallin B chain (P02511) · a predicted model of the same protein · chain A against A, TM-score 0.90

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