2KRG: Na/H exchange regulatory cofactor NHE-RF1

Solution Structure of human sodium/ hydrogen exchange regulatory factor 1(150-358). Determined by solution NMR. Released 29 Dec 2009.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,657
Mol. weight
23.67 kDa
Released
29 Dec 2009

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

Secondary structure: helices and β-sheets

2KRG contains 9 α-helices and 8 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: 9 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand153-15861
β-strand166-16832
β-strand17813
β-strand179-18242
α-helix187-1915
β-strand19813
β-strand201-20221
β-strand205-20621
α-helix213-22210
β-strand225-23061
α-helix233-24210
α-helix248-2514
α-helix269-2713
α-helix275-2773
α-helix297-2993
α-helix323-3286
α-helix331-3333

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Na(+)/H(+) exchange regulatory cofactor NHE-RF1Aprotein216Homo sapiensO14745 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KRG_1 Na(+)/H(+) exchange regulatory cofactor NHE-RF1 (chains A)
GIDPFTMLRPRLCTMKKGPSGYGFNLHSDKSKPGQFIRSVDPDSPAEASGLRAQDRIVEV
NGVCMEGKQHGDVVSAIRAGGDETKLLVVDRETDEFFKKCRVIPSQEHLNGPLPVPFTNG
EIQKENSREALAEAALESPRPALVRSASSDTSEELNSQDSPPKQDSTAPSSTSSSDPILD
FNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL

Primary citation

A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. Bhattacharya, S., Dai, Z., Li, J. et al. J Biol Chem (2010) 285:9981-9994. DOI 10.1074/jbc.M109.074005 · PubMed

Other PDB entries of the same protein (UniProt O14745 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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