Research workbench

The monomeric ASP49 secretory phospholipase A2 from the venom of agkistridon piscivorus piscivorus

Analyse The monomeric ASP49 secretory phospholipase A2 from the venom of agkistridon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VAP
Type: protein
Length: 246 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2
EC: 3.1.1.4
UniProt: P51972
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phospholipase A2 (EC 3.1.1.4)	protein	123	48% helix, 11% strand	P51972

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	172	0.54	0.79	25	empty
2	132	0.53	0.81	20	empty

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

1VAP · The monomeric ASP49 secretory phospholipase A2 from the venom of agkistridon piscivorus… · the same entry in another collection · chain A against A, TM-score 1.00
P51972 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 app-D49 (P51972) · 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 P51972
Elsewhere: RCSB PDB 1VAP · PDBe 1VAP · UniProt P51972

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.