MolNFT v1 · #88740 · protein

Crystal structure of glucose-1-phosphate uridylyltransferase galu from erwinia amylovora.

4D48: “Crystal structure of glucose-1-phosphate uridylyltransferase galu from erwinia amylovora.”. X-ray diffraction, 6 pockets (best druggability 0.66). MolNFT v1 #88740 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4D48
Type: protein
Length: 569 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-1-phosphate uridylyltransferase
EC: 2.7.7.9
UniProt: D4I3X5
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9)	protein	284	35% helix, 23% strand	D4I3X5
B	Glucose-1-phosphate uridylyltransferase (EC 2.7.7.9)	protein	285	34% helix, 22% strand	D4I3X5

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	652	0.66	0.75	61	empty
2	641	0.66	0.75	55	empty
3	293	0.61	0.79	45	empty
4	164	0.46	0.76	30	empty
5	101	0.39	0.76	21	empty

Interfaces

1 interface between chains.

A–B · 2208 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4D48 · Crystal Structure of glucose-1-phosphate uridylyltransferase GalU from Erwinia amylovora. · 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 D4I3X5
Elsewhere: RCSB PDB 4D48 · PDBe 4D48 · UniProt D4I3X5

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