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Structure of E. COLI uridine phosphorylase at 2.0A

Analyse Structure of E. COLI uridine phosphorylase at 2.0A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LX7
Type: protein
Length: 471 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uridine phosphorylase
EC: 2.4.2.3
UniProt: P12758
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uridine phosphorylase (EC 2.4.2.3)	protein	250	35% helix, 29% strand	P12758
B	Uridine phosphorylase (EC 2.4.2.3)	protein	221	35% helix, 31% strand	P12758

Pockets

3 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	482	0.72	0.81	44	empty
2	283	0.60	0.79	29	empty
3	52	0.26	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 1457 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

1LX7 · Structure of E. coli uridine phosphorylase at 2.0A · the same entry in another collection · chain A against A, TM-score 1.00
P12758 · AlphaFold monomer V2.0 prediction for uridine phosphorylase (P12758) · a predicted model of the same protein · chain B 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 P12758
Elsewhere: RCSB PDB 1LX7 · PDBe 1LX7 · UniProt P12758

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