MolNFT v1 · #163348 · protein

Crystal structure of methionine gamma-lyase from citrobacter freundii modified by dimethylthiosulfinate

6S0C · Cystathionine gamma-synthase: “Crystal structure of methionine gamma-lyase from citrobacter freundii modified by dimethylthiosulfinate”. X-ray diffraction, 1 ligand (PLP), 2 pockets (best druggability 0.62). MolNFT v1 #163348 on…

PDB: 6S0C
Type: protein
Length: 390 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cystathionine gamma-synthase
EC: 4.4.1.11
UniProt: A0A0A5P8W7
Ligands: PLP
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cystathionine gamma-synthase (EC 4.4.1.11)	protein	390	41% helix, 16% strand	A0A0A5P8W7

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · chains A
PGE · Triethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	313	0.62	0.79	42	PLP
2	82	0.32	0.74	24	empty

Modifications

Observed in the structure: 3 modified, 1 cofactor (methylation, pyridoxal phosphate Schiff base).

Compared structures

6S0C · Crystal structure of methionine gamma-lyase from Citrobacter freundii modified by… · 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 A0A0A5P8W7
Elsewhere: RCSB PDB 6S0C · PDBe 6S0C · UniProt A0A0A5P8W7

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