2KSA: Substance-P receptor

Substance P in DMPC/CHAPS isotropic q=0.25 bicelles as a ligand for NK1R. Determined by solution NMR. Released 3 Nov 2010.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
3,023
Mol. weight
43.03 kDa
Released
3 Nov 2010

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

Secondary structure: helices and β-sheets

2KSA contains 13 α-helices and 2 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: 12 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix29-5931
α-helix66-8015
α-helix81-855
α-helix86-9510
α-helix102-13534
α-helix144-16219
β-strand17311
β-strand18011
α-helix193-1997
α-helix200-2067
α-helix207-22115
α-helix238-27336
α-helix284-30825
α-helix310-32011
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix369-3724

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Substance-P receptorAprotein364Homo sapiensP25103 (AlphaFold model)
Substance PBprotein11P20366 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KSA_1 Substance-P receptor (chains A)
MDNVLPVDSDLSPNISTNTSEPNQFVQPAWQIVLWAAAYTVIVVTSVVGNVVVMWIILAH
KRMRTVTNYFLVNLAFAEASMAAFNTVVNFTYAVHNEWYYGLFYCKFHNFFPIAAVFASI
YSMTAVAFDRYMAIIHPLQPRLSATATKVVICVIWVLALLLAFPQGYYSTTETMPSRVVC
MIEWPEHPNKIYEKVYHICVTVLIYFLPLLVIGYAYTVVGITLWASEIPGDSSDRYHEQV
SAKRKVVKMMIVVVCTFAICWLPFHIFFLLPYINPDLYLKKFIQQVYLAIMWLAMSSTMY
NPIIYCCLNDRFRLGFKHAFRCCPFISAGDYEGLEMKSTRYLQTQGSVYKVSRLETTIST
VVGA
Sequence of entity 2 (B), FASTA
>2KSA_2 Substance P (chains B)
RPKPQQFFGLM

Primary citation

NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles. Gayen, A., Goswami, S.K., Mukhopadhyay, C. Biochim Biophys Acta (2010). DOI 10.1016/j.bbamem.2010.09.023 · PubMed

Other PDB entries of the same protein (UniProt P25103 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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