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Roll out the beta-barrel: structure and mechanism of PAC13, a unique nucleoside dehydratase

Analyse Roll out the beta-barrel: structure and mechanism of PAC13, a unique nucleoside… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NJO
Type: protein
Length: 121 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative CUPIN_2 domain-containing isomerase
UniProt: E2EKP5
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative CUPIN_2 domain-containing isomerase	protein	121	5% helix, 58% strand	E2EKP5

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.59	0.84	25	empty

Compared structures

5NJO · Roll out the beta-barrel: structure and mechanism of Pac13, a unique nucleoside… · 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 E2EKP5
Elsewhere: RCSB PDB 5NJO · PDBe 5NJO · UniProt E2EKP5

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