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ATP phosphoribosyltransferase (ATP-prtase) from mycobacterium tuberculosis in complex with AMP and histidine

Analyse ATP phosphoribosyltransferase (ATP-prtase) from mycobacterium tuberculosis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NH8
Type: protein
Length: 276 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: Mycobacterium tuberculosis H37Rv
Molecule: ATP Phosphoribosyltransferase
EC: 2.4.2.17
UniProt: P60759
Ligands: AMP, HIS, SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · resolution 1.8 · 1 distinct chain · 32% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP Phosphoribosyltransferase (EC 2.4.2.17)	protein	276	32% helix, 34% strand	P60759

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
HIS · Histidine · ligand · chains A
SO4 · Sulfate ion · ion · 3 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	200	0.48	0.75	34	empty

Compared structures

1NH8 · ATP phosphoribosyltransferase (ATP-prtase) from mycobacterium tuberculosis in complex… · 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 P60759
Elsewhere: RCSB PDB 1NH8 · PDBe 1NH8 · UniProt P60759

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