1MRV: Inactive Akt2 kinase domain

crystal structure of an inactive Akt2 kinase domain. Determined by X-ray diffraction at 2.8 Å resolution. Released 23 Sept 2003.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
1
Atoms
2,150
Mol. weight
39.31 kDa
Released
23 Sept 2003

Explore 1MRV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MRV contains 16 α-helices and 9 β-strands across 1 chain. 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: 16 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix149-1513
β-strand152-161101
β-strand164-17181
β-strand177-18481
β-strand21212
α-helix213-2142
β-strand215-22061
β-strand224-23071
β-strand23612
α-helix237-2448
α-helix249-26719
α-helix278-2803
β-strand281-28332
β-strand289-29132
α-helix319-3235
α-helix330-34516
α-helix355-3573
α-helix358-3647
α-helix366-3683
α-helix375-38410
α-helix400-4045
α-helix407-4093
α-helix414-4174
α-helix423-4242
α-helix437-4393

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RAC-beta serine/threonine kinaseAprotein339Homo sapiensP31751 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1MRV_1 RAC-beta serine/threonine kinase (chains A)
ARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESR
VLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSA
LEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVL
EDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLA
GLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDE
FTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE

Primary citation

Crystal structure of an inactive akt2 kinase domain. Huang, X., Begley, M., Morgenstern, K.A. et al. Structure (2003) 11:21-30. DOI 10.1016/S0969-2126(02)00937-1 · PubMed

Other PDB entries of the same protein (UniProt P31751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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