2WT8: N-terminal BRCT domain of human microcephalin

Structure of the N-terminal BRCT domain of human microcephalin (Mcph1). Determined by X-ray diffraction at 1.6 Å resolution. Released 1 Dec 2009.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
3,433
Mol. weight
43.43 kDa
Released
1 Dec 2009

Explore 2WT8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WT8 contains 20 α-helices and 28 β-strands across 4 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: 5 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix1-44
β-strand10-1561
β-strand1612
β-strand2312
α-helix25-3410
β-strand38-3921
β-strand49-5351
α-helix57-6610
β-strand69-7131
α-helix73-8210
α-helix88-903
β-strand9211
Chain B: 5 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix2-43
β-strand10-1563
β-strand1614
β-strand2314
α-helix25-3410
β-strand38-3923
β-strand49-5353
α-helix57-6610
β-strand69-7133
α-helix73-8210
α-helix88-903
β-strand9213
Chain C: 4 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand10-1565
β-strand1616
β-strand2316
α-helix25-3410
β-strand38-3925
β-strand49-5355
α-helix57-6610
β-strand69-7135
α-helix73-8210
α-helix88-903
β-strand9215
Chain D: 6 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand10-1567
β-strand1618
β-strand2318
α-helix25-284
α-helix29-335
β-strand38-4037
β-strand49-5357
α-helix57-6610
α-helix681
β-strand69-7137
α-helix73-8210
α-helix88-903
β-strand9217

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MicrocephalinA, B, C, Dprotein97HOMO SAPIENSQ8NEM0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2WT8_1 MICROCEPHALIN (chains A, B, C, D)
GAMAAPILKDVVAYVEVWSSNGTENYSKTFTTQLVDMGAKVSKTFNKQVTHVIFKDGYQS
TWDKAQKRGVKLVSVLWVEKCRTAGAHIDESLFPAAN

Primary citation

A Pocket on the Surface of the N-Terminal Brct Domain of Mcph1 is Required to Prevent Abnormal Chromosome Condensation. Richards, M.W., Leung, J.W.C., Roe, S.M. et al. J Mol Biol (2010) 395:908. DOI 10.1016/J.JMB.2009.11.029 · PubMed

Other PDB entries of the same protein (UniProt Q8NEM0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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