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5'-nucleotidase from E. COLI

Analyse 5'-nucleotidase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1USH
Type: protein
Length: 515 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5'-nucleotidase
EC: 3.1.3.5
UniProt: P07024
Ligands: ZN, SO4, CO3
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5'-nucleotidase (EC 3.1.3.5)	protein	515	29% helix, 30% strand	P07024

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
CO3 · Carbonate ion · ion · 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	901	0.74	0.78	107	CO3
2	65	0.29	0.73	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1USH · 5'-nucleotidase from E. COLI · the same entry in another collection · chain A against A, TM-score 1.00
P07024 · AlphaFold monomer V2.0 prediction for protein usha (P07024) · a predicted model of the same protein · chain A against A, TM-score 0.73

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 P07024
Elsewhere: RCSB PDB 1USH · PDBe 1USH · UniProt P07024

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