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Crystal structure of mouse cytosolic sulfotransferase MSULT2A8 in complex with pap and cholic acid

Analyse Crystal structure of mouse cytosolic sulfotransferase MSULT2A8 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EOV
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosolic sulfotransferase SULT2A8
EC: 2.8.2.-
UniProt: Q8BGL3
Ligands: CHD, A3P
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytosolic sulfotransferase SULT2A8 (EC 2.8.2.-)	protein	274	48% helix, 10% strand	Q8BGL3

Ligands and binding sites

CHD · Cholic acid · ligand · 2 copies · chains A
A3P · Adenosine-3'-5'-diphosphate · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	470	0.80	0.87	48	A3P, CHD
2	99	0.53	0.83	14	empty

Compared structures

7EOV · Crystal structure of mouse cytosolic sulfotransferase mSULT2A8 in complex with PAP and… · 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 Q8BGL3
Elsewhere: RCSB PDB 7EOV · PDBe 7EOV · UniProt Q8BGL3

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