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Triphosphate tunnel metalloenzyme from Sulfolobus acidocaldarius

Analyse Triphosphate tunnel metalloenzyme from Sulfolobus acidocaldarius in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NS8
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.3
Source: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157…
Molecule: Triphosphate tunnel metalloenzyme Saci_0718
UniProt: Q4JAT2
Ligands: SO4
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 28% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triphosphate tunnel metalloenzyme Saci_0718	protein	162	28% helix, 48% strand	Q4JAT2

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
CXS · 3-cyclohexyl-1-propylsulfonic acid · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	203	0.45	0.74	34	SO4

Compared structures

7NS8 · Triphosphate tunnel metalloenzyme from sulfolobus acidocaldarius · 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 Q4JAT2
Elsewhere: RCSB PDB 7NS8 · PDBe 7NS8 · UniProt Q4JAT2

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