MolNFT v1 · #22024 · protein

Serine acetyltransferase- complex with CoA

1SST: “Serine acetyltransferase- complex with CoA”. X-ray diffraction, 1 ligand (COA), 5 pockets (best druggability 0.77). MolNFT v1 #22024 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1SST
Type: protein
Length: 704 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine acetyltransferase
EC: 2.3.1.30
UniProt: P43886
Ligands: COA
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine acetyltransferase (EC 2.3.1.30)	protein	233	46% helix, 16% strand	P43886
B	Serine acetyltransferase (EC 2.3.1.30)	protein	235	45% helix, 15% strand	P43886
C	Serine acetyltransferase (EC 2.3.1.30)	protein	236	46% helix, 17% strand	P43886

Ligands and binding sites

COA · Coenzyme A · ligand · 3 copies · chains A, B, C

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

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	443	0.77	0.86	41	empty
2	100	0.76	0.97	26	empty
3	561	0.73	0.81	72	COA
4	550	0.71	0.80	68	COA
5	470	0.70	0.80	74	COA

Interfaces

3 interfaces between chains.

A–B · 1217 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 1192 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 1182 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1SST · Serine Acetyltransferase- Complex with CoA · the same entry in another collection · chain A against A, TM-score 1.00
P43886 · AlphaFold monomer V2.0 prediction for serine acetyltransferase (P43886) · a predicted model of the same protein · chain B 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 P43886
Elsewhere: RCSB PDB 1SST · PDBe 1SST · UniProt P43886

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