Research workbench

Hallucinated C3 protein assembly HALC3_104

Analyse Hallucinated C3 protein assembly HALC3_104 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8D06
Type: protein
Length: 777 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.4
Source: synthetic construct
Molecule: HALC3_104
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · resolution 3.4 · 7 distinct chains · 87% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, H	HALC3_104	protein	64	84% helix, 0% strand	—
B, C, L	HALC3_104	protein	67	88% helix, 0% strand	—
D	HALC3_104	protein	65	86% helix, 0% strand	—
E, F, K	HALC3_104	protein	66	88% helix, 0% strand	—
G	HALC3_104	protein	60	83% helix, 0% strand	—
I	HALC3_104	protein	59	92% helix, 0% strand	—
J	HALC3_104	protein	66	85% helix, 0% strand	—

Pockets

4 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	976	0.76	0.78	55	empty
2	649	0.68	0.77	56	empty
3	56	0.40	0.81	15	empty
4	110	0.34	0.73	17	empty

Interfaces

18 interfaces between chains.

A–B · 1026 Å² buried · 10 hydrogen bonds · protein-protein
K–J · 989 Å² buried · 9 hydrogen bonds · protein-protein
D–E · 986 Å² buried · 4 hydrogen bonds · protein-protein
L–J · 978 Å² buried · 8 hydrogen bonds · protein-protein
L–K · 976 Å² buried · 8 hydrogen bonds · protein-protein

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 8D06 · PDBe 8D06

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