Research workbench

Crystal structure of phospholipase A2 from daboia russelli pulchella

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

PDB: 1CL5
Type: protein
Length: 242 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (phospholipase A2)
EC: 3.1.1.4
UniProt: P59071
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (phospholipase A2) (EC 3.1.1.4)	protein	121	47% helix, 9% strand	P59071

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	192	0.73	0.89	24	empty
2	208	0.69	0.87	33	empty
3	123	0.54	0.82	19	empty
4	63	0.35	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 751 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

1CL5 · Crystal structure of phospholipase A2 from daboia russelli pulchella · 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 1CL5 · PDBe 1CL5 · UniProt P59071

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