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Staphylococcus aureus adenylosuccinate lyase

Analyse Staphylococcus aureus adenylosuccinate lyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X75
Type: protein
Length: 427 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: STAPHYLOCOCCUS AUREUS
Molecule: Adenylosuccinate lyase
EC: 4.3.2.2
UniProt: C8LPI8
Ligands: OXL, AMP, CL
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · resolution 2.5 · 1 distinct chain · 62% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylosuccinate lyase (EC 4.3.2.2)	protein	427	62% helix, 5% strand	C8LPI8

Ligands and binding sites

OXL · Oxalate ion · ligand · chains A
AMP · Adenosine monophosphate · ligand · chains A
CL · Chloride ion · ion · chains A
P6G · Hexaethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.62	0.85	27	empty
2	59	0.39	0.80	13	empty

Compared structures

2X75 · Staphylococcus aureus adenylosuccinate lyase · 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 C8LPI8
Elsewhere: RCSB PDB 2X75 · PDBe 2X75 · UniProt C8LPI8

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