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Haemonchus galactose containing glycoprotein complex

Analyse Haemonchus galactose containing glycoprotein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ROW
Type: protein
Length: 3,129 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative zinc metallopeptidase; Parasite pepsinogen; Cysteine protease
UniProt: O76751, Q25037
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 7 distinct chains · 42% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative zinc metallopeptidase	protein	596	53% helix, 3% strand	O76751
B	Putative zinc metallopeptidase	protein	619	51% helix, 3% strand	O76751
C	Putative zinc metallopeptidase	protein	583	49% helix, 4% strand	O76751
D	Putative zinc metallopeptidase	protein	566	54% helix, 3% strand	O76751
E	Parasite pepsinogen	protein	299	8% helix, 25% strand	Q25037
F	Parasite pepsinogen	protein	293	10% helix, 20% strand	Q25037
G	Cysteine protease	protein	173	25% helix, 10% strand	—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	752	0.85	0.88	113	empty
2	700	0.82	0.86	119	empty
3	699	0.82	0.86	125	empty
4	894	0.81	0.84	118	empty
5	927	0.81	0.83	101	empty

Interfaces

5 interfaces between chains.

A–B · 1143 Å² buried · 4 hydrogen bonds · protein-protein
C–D · 1110 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 393 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 342 Å² buried · 2 hydrogen bonds · protein-protein
B–G · 213 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 17 disulfide (disulfide).

Compared structures

6ROW · Haemonchus galactose containing glycoprotein complex · 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 O76751
Every structure of UniProt Q25037
Elsewhere: RCSB PDB 6ROW · PDBe 6ROW · UniProt O76751 · UniProt Q25037

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