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Crystal structure of M120A mutant of O-acetylserine sulfhydrylase from haemophilus influenzae in complex with high affinity inhibitory peptide from serine acetyl transferase of salmonella typhimurium

Analyse Crystal structure of M120A mutant of O-acetylserine sulfhydrylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6AIF
Type
protein
Length
318 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cysteine synthase; Peptide from serine acetyltransferase
EC
2.5.1.47
UniProt
P45040, P29847
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACysteine synthase (EC 2.5.1.47)protein31041% helix, 18% strandP45040
BPeptide from serine acetyltransferaseprotein80% helix, 13% strandP29847

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11150.510.8124empty
2800.390.7722empty

Interfaces

1 interface between chains.

  • A–B · 592 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

  • 6AIF · Crystal structure of M120A mutant of O-acetylserine sulfhydrylase from Haemophilus… · the same entry in another collection · chain A against A, TM-score 1.00
  • P45040 · AlphaFold monomer V2.0 prediction for cysteine synthase (P45040) · a predicted model of the same protein · chain A against A, TM-score 1.00
  • P29847 · AlphaFold monomer V2.0 prediction for serine acetyltransferase (P29847) · a predicted model of the same protein · chain B against A, TM-score 0.37

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