3N1O: IhhN

Crystal structure of IhhN. Determined by X-ray diffraction at 2.55 Å resolution. Released 2 Jun 2010.

Method
X-ray diffraction
Resolution
2.55 Å
Organism
Homo sapiens
Chains
3
Atoms
3,753
Mol. weight
57.6 kDa
Ligands
ZN, CA
Released
2 Jun 2010

Explore 3N1O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3N1O contains 20 α-helices and 24 β-strands across 3 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: 7 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix45-484
β-strand52-5321
α-helix76-805
β-strand82-8322
β-strand89-9131
α-helix99-1013
β-strand102-10322
α-helix105-12117
β-strand127-13151
α-helix144-1474
β-strand150-15561
α-helix160-1623
α-helix163-17210
β-strand177-18261
β-strand185-18951
Chain B: 6 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix46-483
β-strand52-5323
α-helix76-805
β-strand82-8324
β-strand89-9133
α-helix99-1013
β-strand102-10324
α-helix105-12117
β-strand127-13153
α-helix144-1474
β-strand150-15563
α-helix163-17210
β-strand177-17933
β-strand186-18943
Chain C: 7 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix45-484
β-strand52-5325
α-helix77-804
β-strand82-8326
β-strand89-9135
α-helix99-1013
β-strand102-10326
α-helix105-12117
β-strand127-13155
α-helix144-1474
β-strand150-15565
α-helix160-1623
α-helix163-17210
β-strand177-17935
β-strand186-18945

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Indian hedgehog proteinA, B, Cprotein169Homo sapiensQ14623 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>3N1O_1 Indian hedgehog protein (chains A, B, C)
GSGPGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPN
YNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESL
HYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn3
CACalcium ionCa1

Primary citation

All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner. Kavran, J.M., Ward, M.D., Oladosu, O.O. et al. J Biol Chem (2010) 285:24584-24590. DOI 10.1074/jbc.M110.131680 · PubMed

Other PDB entries of the same protein (UniProt Q14623 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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