MolNFT v1 · #99739 · protein

Crystal structure of uridine phosphorylase from vibrio fischeri ES114 complexed with 6-hydroxy-1-naphthoic acid, nysgrc target 029520.

4MCH: “Crystal structure of uridine phosphorylase from vibrio fischeri ES114 complexed with 6-hydroxy-1-naphthoic…”. X-ray diffraction, 2 ligands (61N, SO4), 1 pocket (best druggability 0.47). MolNFT v1 #99739 on GenesisL1: 3D structure…

PDB: 4MCH
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uridine phosphorylase
EC: 2.4.2.3
UniProt: Q5E046
Ligands: 61N, SO4
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uridine phosphorylase (EC 2.4.2.3)	protein	243	37% helix, 30% strand	Q5E046

Ligands and binding sites

61N · 6-hydroxynaphthalene-1-carboxylic acid · ligand · chains A
SO4 · Sulfate ion · ion · chains A
DMS · Dimethyl sulfoxide · additive · 14 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	166	0.47	0.76	29	SO4, DMS

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

4MCH · Crystal structure of uridine phosphorylase from vibrio fischeri es114 complexed with… · 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 Q5E046
Elsewhere: RCSB PDB 4MCH · PDBe 4MCH · UniProt Q5E046

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