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Crystal structure of adenylosuccinate lyase (asl) from pseudomonas aeruginosa complexed with AMP

Analyse Crystal structure of adenylosuccinate lyase (asl) from pseudomonas aeruginosa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7T29
Type: protein
Length: 453 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylosuccinate lyase
EC: 4.3.2.2
UniProt: Q9I0K9
Ligands: AMP
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylosuccinate lyase (EC 4.3.2.2)	protein	453	64% helix, 5% strand	Q9I0K9

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
EDO · 1,2-ethanediol · additive · 2 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	87	0.40	0.77	14	empty

Compared structures

7T29 · Crystal Structure of Adenylosuccinate lyase (ASL) from Pseudomonas aeruginosa complexed… · the same entry in another collection · chain A against A, TM-score 1.00
Q9I0K9 · AlphaFold monomer V2.0 prediction for adenylosuccinate lyase (Q9I0K9) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9I0K9
Elsewhere: RCSB PDB 7T29 · PDBe 7T29 · UniProt Q9I0K9

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