Research workbench

HICA3 and HICB3 toxin-antitoxin complex

Analyse HICA3 and HICB3 toxin-antitoxin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4P78
Type: protein
Length: 304 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HICB3 antitoxin; HICA3 toxin
UniProt: Q0WBS6, Q74XS2
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HICB3 antitoxin	protein	86	38% helix, 27% strand	Q0WBS6
C, D	HICA3 toxin	protein	66	32% helix, 35% strand	Q74XS2

Ligands and binding sites

GOL · Glycerol · additive · chains B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.44	0.83	13	empty
2	77	0.35	0.76	14	empty

Interfaces

3 interfaces between chains.

A–D · 1414 Å² buried · 34 hydrogen bonds · protein-protein
B–C · 1379 Å² buried · 31 hydrogen bonds · protein-protein
A–B · 981 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4P78 · HicA3 and HicB3 toxin-antitoxin 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 Q0WBS6
Every structure of UniProt Q74XS2
Elsewhere: RCSB PDB 4P78 · PDBe 4P78 · UniProt Q0WBS6 · UniProt Q74XS2

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