GL1X · GenesisL1 explorer

Research workbench

Crystal structures of cystathionine beta-synthase from saccharomyces cerevisiae: the structure of the pmp complex

Analyse Crystal structures of cystathionine beta-synthase from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C4P
Type
protein
Length
344 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cystathionine beta-synthase
EC
4.2.1.22
UniProt
P32582
Ligands
PMP, CA, NA, CL
Pockets
2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACystathionine beta-synthase (EC 4.2.1.22)protein34440% helix, 17% strandP32582

Ligands and binding sites

  • PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A
  • CA · Calcium ion · metal · chains A
  • NA · Sodium ion · metal · chains A
  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12850.780.9049PMP, CL
2840.340.7413PEG

Compared structures

  • 6C4P · Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P32582 · AlphaFold monomer V2.0 prediction for cystathionine beta-synthase (P32582) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.