MolNFT v1 · #78984 · protein

Crystal structure of O-acetyl serine sulfhydrylase from leishmania donovani

3SPX: “Crystal structure of O-acetyl serine sulfhydrylase from leishmania donovani”. X-ray diffraction, 2 ligands (NA, CL), 3 pockets (best druggability 0.66). MolNFT v1 #78984 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3SPX
Type: protein
Length: 320 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O-acetyl serine sulfhydrylase
EC: 2.5.1.47
UniProt: G1C2I2
Ligands: NA, CL
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	O-acetyl serine sulfhydrylase (EC 2.5.1.47)	protein	320	43% helix, 18% strand	G1C2I2

Ligands and binding sites

NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	441	0.66	0.79	40	empty
2	114	0.53	0.82	19	empty
3	55	0.33	0.77	14	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

3SPX · Crystal structure of O-Acetyl Serine Sulfhydrylase from Leishmania donovani · the same entry in another collection · chain A against A, TM-score 1.00

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 G1C2I2
Elsewhere: RCSB PDB 3SPX · PDBe 3SPX · UniProt G1C2I2

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