MolNFT v1 · #28584 · protein

Structural genomics of caenorhabditis elegans: adenylosuccinate lyase

1YIS: “Structural genomics of caenorhabditis elegans: adenylosuccinate lyase”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.62). MolNFT v1 #28584 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1YIS
Type: protein
Length: 421 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenylosuccinate lyase
EC: 4.3.2.2
UniProt: Q21774
Ligands: SO4
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenylosuccinate lyase (EC 4.3.2.2)	protein	421	69% helix, 5% strand	Q21774

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	248	0.62	0.81	31	empty
2	76	0.39	0.78	18	empty

Modifications

Observed in the structure: 10 modified, 1 disulfide (engineered, disulfide).

Compared structures

1YIS · Structural genomics of Caenorhabditis elegans: adenylosuccinate lyase · the same entry in another collection · chain A against A, TM-score 1.00
Q21774 · AlphaFold monomer V2.0 prediction for adenylosuccinate lyase (Q21774) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q21774
Elsewhere: RCSB PDB 1YIS · PDBe 1YIS · UniProt Q21774

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