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Carboxylic ester hydrolase, 1.72 ångström trigonal form of the bovine recombinant PLA2 enzyme

Analyse Carboxylic ester hydrolase, 1.72 ångström trigonal form of the bovine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MKT
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2
EC: 3.1.1.4
UniProt: P00593
Ligands: CA
Pockets: 1 · best druggability 0.64

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipase A2 (EC 3.1.1.4)	protein	123	47% helix, 9% strand	P00593

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	108	0.64	0.88	17	empty

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

1MKT · Carboxylic ester hydrolase, 1.72 ångström trigonal form of the bovine recombinant PLA2… · the same entry in another collection · chain A against A, TM-score 1.00
P00593 · AlphaFold monomer V2.0 prediction for phospholipase A2 (P00593) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P00593
Elsewhere: RCSB PDB 1MKT · PDBe 1MKT · UniProt P00593

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