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Anticoagulant class II phospholipase A2 from the venom of vipera russelli russelli

Analyse Anticoagulant class II phospholipase A2 from the venom of vipera russelli… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VIP
Type: protein
Length: 121 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2
EC: 3.1.1.4
UniProt: P81458
Ligands: SO4
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipase A2 (EC 3.1.1.4)	protein	121	49% helix, 9% strand	P81458

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

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	144	0.45	0.76	18	empty

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

1VIP · Anticoagulant class II phospholipase A2 from the venom of vipera russelli russelli · the same entry in another collection · chain A against A, TM-score 1.00
P81458 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 rvv-vd (P81458) · 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 P81458
Elsewhere: RCSB PDB 1VIP · PDBe 1VIP · UniProt P81458

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