MolNFT v1 · #91538 · protein

Design of peptide inhibitors of group II phospholipase A2: crystal structure of the complex of phospholipsae A2 with a designed tripeptide, ala- tyr- lys at 2.3 a resolution

4FGA · Phospholipase A2 vrv-pl-viiia: “Design of peptide inhibitors of group II phospholipase A2: crystal structure of the complex of phospholipsae…”. X-ray diffraction, 1 pocket (best druggability 0.35). MolNFT v1 #91538 on GenesisL1: 3D…

PDB: 4FGA
Type: protein
Length: 124 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2 vrv-pl-viiia; Ayk
EC: 3.1.1.4
UniProt: D0VX11
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipase A2 vrv-pl-viiia (EC 3.1.1.4)	protein	121	48% helix, 8% strand	D0VX11
P	Ayk	protein	3	0% helix, 0% strand	—

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	72	0.35	0.76	13	empty

Interfaces

1 interface between chains.

A–P · 397 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

4FGA · Design of peptide inhibitors of group II phospholipase A2: Crystal structure of the… · 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 4FGA · PDBe 4FGA · UniProt D0VX11

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