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Crystal structure of anaerobic ergothioneine biosynthesis enzyme from chlorobium limicola in complex with natural substrate trimethyl histidine.

Analyse 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: 6H9A
Type: protein
Length: 425 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulfurtransferase
UniProt: B3ECE3
Ligands: AVJ, NA, CL, SO4
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulfurtransferase	protein	425	33% helix, 18% strand	B3ECE3

Ligands and binding sites

AVJ · N,N,N-trimethyl-histidine · ligand · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A
SO4 · Sulfate ion · ion · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.68	0.94	20	AVJ
2	194	0.53	0.79	26	empty
3	129	0.48	0.79	25	CL
4	136	0.39	0.74	22	CL

Compared structures

6H9A · Crystal structure of anaerobic ergothioneine biosynthesis enzyme from Chlorobium limicola… · the same entry in another collection · chain A against A, TM-score 1.00

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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 6H9A · PDBe 6H9A · UniProt B3ECE3

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