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Crystal structure of the complex of phospholipase A2 with gramine derivative at 1.80 a resolution

Analyse Crystal structure of the complex of phospholipase A2 with gramine derivative at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QGD
Type: protein
Length: 121 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2 vrv-pl-viiia
EC: 3.1.1.4
UniProt: D0VX11
Ligands: PZZ
Pockets: 1 · best druggability 0.49

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipase A2 vrv-pl-viiia (EC 3.1.1.4)	protein	121	48% helix, 7% strand	D0VX11

Ligands and binding sites

PZZ · 3-{3-[(dimethylamino)methyl]-1H-indol-7-yl}propan-1-ol · ligand · 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	114	0.49	0.80	20	PZZ

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

4QGD · Crystal Structure of the Complex of Phospholipase A2 with Gramine derivative at 1.80 A… · the same entry in another collection · chain A against A, TM-score 1.00

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 D0VX11
Elsewhere: RCSB PDB 4QGD · PDBe 4QGD · UniProt D0VX11

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