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An anti-parallel four helix bundle

Analyse An anti-parallel four helix bundle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W5K
Type: protein
Length: 132 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: General control protein GCN4
UniProt: P03069
Ligands: TYZ

Structure

x-ray diffraction · 1 distinct chain · 91% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	General control protein GCN4	protein	33	91% helix, 0% strand	P03069

Ligands and binding sites

TYZ · Para acetamido benzoic acid · ligand · chains A, B, C

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

Interfaces

4 interfaces between chains.

C–D · 770 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 769 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 101 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 74 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

1W5K · An anti-parallel four helix bundle · the same entry in another collection · chain D against D, TM-score 1.00
P03069 · AlphaFold monomer V2.0 prediction for general control transcription factor GCN4 (P03069) · a predicted model of the same protein · chain D against A, TM-score 0.93

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 P03069
Elsewhere: RCSB PDB 1W5K · PDBe 1W5K · UniProt P03069

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