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Native crystal structure of anaerobic ergothioneine biosynthesis enzyme from chlorobium limicola.

Analyse Native crystal structure of anaerobic ergothioneine biosynthesis enzyme from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6H98
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulfurtransferase
UniProt: B3ECE3
Ligands: MG, CL
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulfurtransferase	protein	424	34% helix, 17% strand	B3ECE3

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A
CL · Chloride ion · ion · chains A
FMT · Formic acid · additive · chains A
EOH · Ethanol · additive · chains A
GOL · Glycerol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.52	0.79	23	empty
2	90	0.43	0.79	21	CL
3	128	0.38	0.73	23	EOH

Compared structures

6H98 · Native crystal structure of anaerobic ergothioneine biosynthesis enzyme from Chlorobium… · 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 B3ECE3
Elsewhere: RCSB PDB 6H98 · PDBe 6H98 · UniProt B3ECE3

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