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Structure of O-acetylserine sulfhydrylase in complex with peptide mnydi

Analyse Structure of O-acetylserine sulfhydrylase in complex with peptide mnydi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IQH
Type
protein
Length
313 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cysteine synthase; Mnydi
EC
2.5.1.47
UniProt
P45040
Ligands
SO4
Pockets
1 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XCysteine synthase (EC 2.5.1.47)protein31043% helix, 17% strandP45040
PMnydiprotein30% helix, 0% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains X, P

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12630.580.7844SO4

Interfaces

1 interface between chains.

  • X–P · 389 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

  • 3IQH · Structure of O-Acetylserine Sulfhydrylase in Complex with Peptide MNYDI · the same entry in another collection · chain X against X, TM-score 1.00
  • P45040 · AlphaFold monomer V2.0 prediction for cysteine synthase (P45040) · a predicted model of the same protein · chain X against A, TM-score 1.00

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