MolNFT v1 · #18416 · protein

Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate

1POD: “Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.55). MolNFT v1 #18416 on GenesisL1: 3D structure, binding sites and…

PDB: 1POD
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2
EC: 3.1.1.4
UniProt: P14555
Ligands: CA
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipase A2 (EC 3.1.1.4)	protein	124	48% helix, 6% strand	P14555

Ligands and binding sites

CA · Calcium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.55	0.83	21	empty

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

1POD · Structures of free and inhibited human secretory phospholipase A2 from inflammatory… · the same entry in another collection · chain A against A, TM-score 1.00
P14555 · AlphaFold monomer V2.0 prediction for phospholipase A2, membrane associated (P14555) · 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 P14555
Elsewhere: RCSB PDB 1POD · PDBe 1POD · UniProt P14555

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