Research workbench

T. maritima adenylosuccinate lyase

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

PDB: 1C3U
Type: protein
Length: 846 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylosuccinate lyase
EC: 4.3.2.2
UniProt: Q9X0I0
Ligands: SO4
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Adenylosuccinate lyase (EC 4.3.2.2)	protein	423	67% helix, 5% strand	Q9X0I0

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	400	0.65	0.79	54	empty
2	157	0.64	0.86	21	empty
3	163	0.63	0.85	24	empty
4	443	0.59	0.75	50	empty

Interfaces

1 interface between chains.

A–B · 1828 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

1C3U · T. maritima adenylosuccinate lyase · the same entry in another collection · chain A against A, TM-score 1.00
Q9X0I0 · AlphaFold monomer V2.0 prediction for adenylosuccinate lyase (Q9X0I0) · 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 Q9X0I0
Elsewhere: RCSB PDB 1C3U · PDBe 1C3U · UniProt Q9X0I0

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