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Structures of toxoplasma gondii MIC2

Analyse Structures of toxoplasma gondii MIC2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OKR
Type: protein
Length: 471 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Micronemal protein MIC2
UniProt: O00816
Ligands: MAN
Pockets: 6 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Micronemal protein MIC2	protein	235	29% helix, 24% strand	O00816
B	Micronemal protein MIC2	protein	236	29% helix, 22% strand	O00816

Ligands and binding sites

MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.56	0.87	17	empty
2	218	0.53	0.77	31	empty
3	99	0.47	0.79	17	empty
4	80	0.46	0.81	17	empty
5	128	0.37	0.73	23	empty

Interfaces

1 interface between chains.

A–B · 387 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 10 disulfide, 2 glycan (disulfide, C-mannosylation).

Compared structures

4OKR · Structures of Toxoplasma gondii MIC2 · 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 O00816
Elsewhere: RCSB PDB 4OKR · PDBe 4OKR · UniProt O00816

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