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Structure of phospholipase A2 from daboia russelli pulchella at 1.95

Analyse Structure of phospholipase A2 from daboia russelli pulchella at 1.95 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FB2
Type: protein
Length: 242 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2
UniProt: P59071
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phospholipase A2	protein	121	48% helix, 8% strand	P59071

Pockets

3 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	593	0.81	0.86	64	empty
2	159	0.58	0.82	25	empty
3	117	0.40	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 562 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

1FB2 · Structure of phospholipase A2 from daboia russelli pulchella at 1.95 · the same entry in another collection · chain A against A, TM-score 1.00
P59071 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 vrv-pl- viiia (P59071) · 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 P59071
Elsewhere: RCSB PDB 1FB2 · PDBe 1FB2 · UniProt P59071

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