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Crystal structure of E.COLI uridine phosphorylase at 2.2 a resolution (type-a native)

Analyse Crystal structure of E.COLI uridine phosphorylase at 2.2 a resolution (type-a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T0U
Type: protein
Length: 474 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: 2 · best druggability 0.65

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	223	35% helix, 32% strand	P12758
B	Uridine phosphorylase (EC 2.4.2.3)	protein	251	34% helix, 29% strand	P12758

Pockets

2 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	377	0.65	0.79	35	empty
2	310	0.58	0.77	37	empty

Interfaces

1 interface between chains.

A–B · 1472 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1T0U · Crystal structure of E.coli uridine phosphorylase at 2.2 A resolution (Type-A Native) · 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 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 P12758
Elsewhere: RCSB PDB 1T0U · PDBe 1T0U · UniProt P12758

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