Research workbench

Crystal structure of the arabidopsis thaliana O-acetylserine sulfhydrylase K46A mutant

Analyse Crystal structure of the arabidopsis thaliana O-acetylserine sulfhydrylase K46A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z7Y
Type: protein
Length: 320 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine synthase
EC: 2.5.1.47
UniProt: P47998
Ligands: AA5
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine synthase (EC 2.5.1.47)	protein	320	43% helix, 17% strand	P47998

Ligands and binding sites

AA5 · N-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine · ligand · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	505	0.74	0.83	51	AA5

Compared structures

1Z7Y · Crystal Structure of the Arabidopsis thaliana O-Acetylserine Sulfhydrylase K46A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P47998 · AlphaFold monomer V2.0 prediction for cysteine synthase 1 (P47998) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P47998
Elsewhere: RCSB PDB 1Z7Y · PDBe 1Z7Y · UniProt P47998

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