1NE4: PDB entry 1NE4

Crystal Structure of Rp-cAMP Binding R1a Subunit of cAMP-dependent Protein Kinase. Determined by X-ray diffraction at 2.4 Å resolution. Released 13 Jan 2004.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Bos taurus
Chains
1
Atoms
2,233
Mol. weight
32.57 kDa
Ligands
RP1
Released
13 Jan 2004

Explore 1NE4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1NE4 contains 16 α-helices and 14 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, 14 β-strands

ElementResiduesLengthSheet
α-helix120-13112
α-helix134-1374
α-helix141-15010
β-strand152-15651
β-strand161-16332
α-helix168-1692
β-strand171-17771
β-strand180-18452
β-strand187-19262
β-strand197-19821
α-helix200-2056
α-helix207-2093
β-strand212-21542
β-strand219-22571
α-helix226-2283
α-helix229-2335
α-helix234-24916
α-helix252-2565
α-helix259-26810
β-strand270-27453
β-strand279-28133
β-strand289-302143
β-strand311-31663
β-strand321-32223
α-helix324-3296
β-strand336-349143
α-helix350-3567
α-helix358-3603
α-helix361-3666
α-helix367-3704

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
cAMP-dependent protein kinase type I-alpha regulatory chainAprotein283Bos taurusP00514 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1NE4_1 cAMP-dependent protein kinase type I-alpha regulatory chain (chains A)
RRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFP
VSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATV
KAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQ
FEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPR
AATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVS

Ligands and cofactors

IDNameFormulaCopies
RP16-(6-amino-purin-9-yl)-2-thioxo-tetrahydro-2-FURO[3,2-D][1,3,2]DIOXAPHOSPHININE…C10 H12 N5 O5 P S2

Primary citation

Crystal Structures of RIalpha Subunit of Cyclic Adenosine 5'-Monophosphate (cAMP)-Dependent Protein Kinase Complexed with (R(p))-Adenosine 3',5'-Cyclic Monophosphothioate and (S(p))-Adenosine 3',5'-Cyclic Monophosphothioate, the Phosphothioate Analogues of cAMP. Wu, J., Jones, J.M., Xuong, N.H. et al. Biochemistry (2004) 43:6620-6629. DOI 10.1021/bi0302503 · PubMed

Other PDB entries of the same protein (UniProt P00514 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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