Research workbench

Crystal structure of a de novo designed antiparallel four-helix coiled coil apcc-tet

Analyse Crystal structure of a de novo designed antiparallel four-helix coiled coil… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Q5S
Type: protein
Length: 120 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apcc-tet
Ligands: ACE, NH2

Structure

x-ray diffraction · 1 distinct chain · 93% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Apcc-tet	protein	30	93% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 3 copies · chains A, D, B, C
NH2 · Amino group · ion · chains C

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

Interfaces

6 interfaces between chains.

B–C · 822 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 810 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 635 Å² buried · 1 hydrogen bond · protein-protein
A–C · 633 Å² buried · 1 hydrogen bond · protein-protein
C–D · 177 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

6Q5S · Crystal structure of a de novo designed antiparallel four-helix coiled coil apCC-Tet · 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 6Q5S · PDBe 6Q5S

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.