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Crystal structure of mouse cytosolic sulfotransferase MSULT1D1 complex with pap and alpha-naphthol

Analyse Crystal structure of mouse cytosolic sulfotransferase MSULT1D1 complex with pap… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZVQ
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-ester sulfotransferase
EC: 2.8.2.9
UniProt: Q9R2C2
Ligands: 1NP, A3P
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Tyrosine-ester sulfotransferase (EC 2.8.2.9)	protein	288	44% helix, 11% strand	Q9R2C2

Ligands and binding sites

1NP · 1-naphthol · ligand · 2 copies · chains X
A3P · Adenosine-3'-5'-diphosphate · ligand · chains X
GOL · Glycerol · additive · 2 copies · chains X

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	301	0.82	0.92	57	A3P, 1NP

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2ZVQ · Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAP and… · the same entry in another collection · chain X against X, 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 Q9R2C2
Elsewhere: RCSB PDB 2ZVQ · PDBe 2ZVQ · UniProt Q9R2C2

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