4AMH: Disks large homolog 1

Influence of circular permutation on the folding pathway of a PDZ domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 5 Dec 2012.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
1,453
Mol. weight
22.96 kDa
Released
5 Dec 2012

Explore 4AMH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AMH contains 5 α-helices and 16 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand17-2151
β-strand2812
β-strand3112
β-strand34-3961
α-helix44-485
β-strand56-6051
β-strand63-6421
α-helix70-789
β-strand83-8971
β-strand97-10371
Chain B: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand17-2153
β-strand2814
β-strand3114
β-strand34-3963
α-helix44-485
α-helix551
β-strand56-6053
β-strand63-6423
α-helix70-789
β-strand83-8973
β-strand98-10363

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Disks large homolog 1A, Bprotein106HOMO SAPIENSQ12959 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4AMH_1 DISKS LARGE HOMOLOG 1 (chains A, B)
MHHHHHLVPRGSKGLGFSIAGGVGNQHWPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAV
NNVALEEVTHEEAVTALKNTSDFVYLKVAKPGSGEKIMEIKLIKGP

Primary citation

Tolerance of Protein Folding to a Circular Permutation in a Pdz Domain. Hultqvist, G., Punekar, A.S., Morrone, A. et al. PLoS One (2012) 7:50055. DOI 10.1371/JOURNAL.PONE.0050055 · PubMed

Other PDB entries of the same protein (UniProt Q12959 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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