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Crystal structure of wild type escherichia COLI adenylosuccinate lyase

Analyse Crystal structure of wild type escherichia COLI adenylosuccinate lyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PTS
Type: protein
Length: 447 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylosuccinate lyase
EC: 4.3.2.2
UniProt: P0AB89
Pockets: 1 · best druggability 0.52

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	447	64% helix, 5% strand	P0AB89

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	174	0.52	0.79	32	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

2PTS · Crystal structure of wild type Escherichia coli adenylosuccinate lyase · the same entry in another collection · chain A against A, TM-score 1.00
P0AB89 · AlphaFold monomer V2.0 prediction for adenylosuccinate lyase (P0AB89) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P0AB89
Elsewhere: RCSB PDB 2PTS · PDBe 2PTS · UniProt P0AB89

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