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Crystal structures of the B1 domain of protein L from peptostreptococcus magnus with a tyrosine to tryptophan substitution

Analyse Crystal structures of the B1 domain of protein L from peptostreptococcus magnus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HZ6
Type
protein
Length
193 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein L
UniProt
Q51912
Pockets
2 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein Lprotein6731% helix, 42% strandQ51912
B, CProtein Lprotein6333% helix, 44% strandQ51912

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.450.8419empty
2680.350.7719empty

Interfaces

3 interfaces between chains.

  • B–C · 594 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 444 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 59 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1HZ6 · Crystal structures of the B1 domain of protein L from peptostreptococcus magnus with a… · the same entry in another collection · chain A against A, TM-score 1.00

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