Research workbench
Influence of circular permutation on the folding pathway of a PDZ domain
Analyse Influence of circular permutation on the folding pathway of a PDZ domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AMH
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disks large homolog 1
- UniProt
- Q12959
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disks large homolog 1 | protein | 94 | 15% helix, 36% strand | Q12959 |
| B | Disks large homolog 1 | protein | 92 | 15% helix, 36% strand | Q12959 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 437 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4AMH · Influence of circular permutation on the folding pathway of a PDZ domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q12959 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q12959) · a predicted model of the same protein · chain B against A, TM-score 0.84
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 Q12959
- Elsewhere: RCSB PDB 4AMH · PDBe 4AMH · UniProt Q12959
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