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The crystal structure of phosphoribosylaminoimidazole carboxylase ATPase subunit of francisella tularensis subsp. tularensis schu S4 in complex with ADP

Analyse The crystal structure of phosphoribosylaminoimidazole carboxylase ATPase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JQW
Type: protein
Length: 365 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N5-carboxyaminoimidazole ribonucleotide synthase
EC: 6.3.4.18
UniProt: Q5NGE8
Ligands: ADP
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N5-carboxyaminoimidazole ribonucleotide synthase (EC 6.3.4.18)	protein	365	35% helix, 28% strand	Q5NGE8

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
ACT · Acetate ion · additive · 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	763	0.74	0.79	64	ADP

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

5JQW · The crystal structure of phosphoribosylaminoimidazole carboxylase ATPase subunit of… · 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 Q5NGE8
Elsewhere: RCSB PDB 5JQW · PDBe 5JQW · UniProt Q5NGE8

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