MolNFT v1 · #53998 · protein

Inhibition of the plp-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation

2XBN: “Inhibition of the plp-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel…”. X-ray diffraction, 2 ligands (PMP, MG), 4 pockets (best druggability 0.42). MolNFT v1 #53998 on GenesisL1: 3D structure…

PDB: 2XBN
Type: protein
Length: 398 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine palmitoyltransferase
UniProt: Q93UV0
Ligands: PMP, MG
Pockets: 4 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine palmitoyltransferase	protein	398	42% helix, 18% strand	Q93UV0

Ligands and binding sites

PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	71	0.42	0.80	17	PMP
2	118	0.40	0.76	21	empty
3	66	0.35	0.77	17	empty
4	63	0.29	0.74	15	empty

Compared structures

2XBN · Inhibition of the PLP-dependent enzyme serine palmitoyltransferase by cycloserine… · 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 Q93UV0
Elsewhere: RCSB PDB 2XBN · PDBe 2XBN · UniProt Q93UV0

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