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Crystal structure analysis of the synthetic GCN4 thioester coiled coil peptide

Analyse Crystal structure analysis of the synthetic GCN4 thioester coiled coil peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3W92
Type: protein
Length: 93 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioester coiled coil peptide
Ligands: TYZ, MCR

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Thioester coiled coil peptide	protein	31	81% helix, 0% strand	—

Ligands and binding sites

TYZ · Para acetamido benzoic acid · ligand · 5 copies · chains A, B, C
MCR · Sulfanylacetic acid · ligand · 3 copies · chains A, B, C
ACT · Acetate ion · additive · 2 copies · chains A, B, C
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Interfaces

3 interfaces between chains.

B–C · 710 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 693 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 640 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 covalent (covalent ligand).

Compared structures

3W92 · Crystal Structure Analysis of the synthetic GCN4 Thioester coiled coil peptide · 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 3W92 · PDBe 3W92

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