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Specific mutations in krait PLA2 lead to dimerization of protein molecules: crystal structure of krait PLA2 at 2.1 resolution

Analyse Specific mutations in krait PLA2 lead to dimerization of protein molecules… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G0Z
Type: protein
Length: 236 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipase A2
EC: 3.1.1.4
Ligands: CL
Pockets: 4 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phospholipase A2 (EC 3.1.1.4)	protein	118	47% helix, 8% strand	—

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	449	0.80	0.87	41	empty
2	90	0.55	0.86	27	empty
3	107	0.54	0.84	30	empty
4	128	0.44	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 867 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

1G0Z · Specific mutations in krait PLA2 lead to dimerization of protein molecules: crystal… · 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
Elsewhere: RCSB PDB 1G0Z · PDBe 1G0Z

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