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Crystal structure of BBBB+UDP+GAL at pH 7.5 with mpd as the cryoprotectant

Analyse Crystal structure of BBBB+UDP+GAL at pH 7.5 with mpd as the cryoprotectant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FRH
Type: protein
Length: 271 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histo-blood group abo system transferase
EC: 2.4.1.37
UniProt: H6A2X0
Ligands: UDP, GAL, MN
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histo-blood group abo system transferase (EC 2.4.1.37)	protein	271	34% helix, 21% strand	H6A2X0

Ligands and binding sites

UDP · Uridine-5'-diphosphate · ligand · chains A
GAL · beta-D-galactopyranose · sugar · chains A
MN · Manganese (II) ion · metal · chains A
PEG · Di(hydroxyethyl)ether · additive · 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	276	0.57	0.77	33	UDP, GAL
2	58	0.38	0.80	15	empty

Compared structures

4FRH · Crystal Structure of BBBB+UDP+Gal at pH 7.5 with MPD as the cryoprotectant · 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 H6A2X0
Elsewhere: RCSB PDB 4FRH · PDBe 4FRH · UniProt H6A2X0

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