Research workbench

Gtb mutant with mercury - E303Q

Analyse Gtb mutant with mercury - E303Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CQP
Type: protein
Length: 265 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histo-blood group abo system transferase
EC: 2.4.1.40, 2.4.1.37
UniProt: P16442
Ligands: HG
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histo-blood group abo system transferase (EC 2.4.1.40, 2.4.1.37)	protein	265	30% helix, 21% strand	P16442

Ligands and binding sites

HG · Mercury (II) ion · metal · 4 copies · 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	221	0.52	0.76	28	HG
2	66	0.30	0.74	16	empty

Compared structures

5CQP · GTB mutant with mercury - E303Q · the same entry in another collection · chain A against A, TM-score 1.00
P16442 · AlphaFold monomer V2.0 prediction for histo-blood group abo system transferase (P16442) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P16442
Elsewhere: RCSB PDB 5CQP · PDBe 5CQP · UniProt P16442

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.