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Crystal structure of aprt from Y. pseudotuberculosis in complex with adenine.

Analyse Crystal structure of aprt from Y. pseudotuberculosis in complex with adenine. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZMI
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenine phosphoribosyltransferase
EC: 2.4.2.7
UniProt: Q66DQ2
Ligands: ADE, NA
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenine phosphoribosyltransferase (EC 2.4.2.7)	protein	178	34% helix, 32% strand	Q66DQ2

Ligands and binding sites

ADE · Adenine · ligand · chains A
NA · Sodium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	236	0.50	0.75	33	ADE

Compared structures

5ZMI · Crystal structure of APRT from Y. pseudotuberculosis in complex with adenine. · the same entry in another collection · chain A against A, TM-score 1.00
Q66DQ2 · AlphaFold monomer V2.0 prediction for adenine phosphoribosyltransferase (Q66DQ2) · 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 Q66DQ2
Elsewhere: RCSB PDB 5ZMI · PDBe 5ZMI · UniProt Q66DQ2

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