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Crystal structure of RV3168 with ATP

Analyse Crystal structure of RV3168 with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ATT
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
UniProt: O53318
Ligands: ATP, MG, CA
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein	protein	352	47% helix, 16% strand	O53318

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CA · Calcium ion · metal · 2 copies · chains A
ACT · Acetate ion · additive · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1060	0.77	0.79	75	MG, ACT, ATP
2	201	0.59	0.81	18	GOL
3	72	0.31	0.74	16	empty
4	54	0.29	0.75	17	empty

Compared structures

3ATT · Crystal structure of Rv3168 with ATP · 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 O53318
Elsewhere: RCSB PDB 3ATT · PDBe 3ATT · UniProt O53318

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