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Crystal structure of bnsp-7, a LYS49-phospholipase A2

Analyse Crystal structure of bnsp-7, a LYS49-phospholipase A2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PA0
Type: protein
Length: 242 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myotoxic phospholipase A2-like
EC: 3.1.1.4
UniProt: Q9IAT9
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Myotoxic phospholipase A2-like (EC 3.1.1.4)	protein	121	48% helix, 7% strand	Q9IAT9

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	155	0.51	0.78	20	empty
2	172	0.51	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 517 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

1PA0 · Crystal structure of bnsp-7, a LYS49-phospholipase A2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9IAT9 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 homolog bnsp-7 (Q9IAT9) · 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 Q9IAT9
Elsewhere: RCSB PDB 1PA0 · PDBe 1PA0 · UniProt Q9IAT9

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