3N1M: IhhN

Crystal Structure of IhhN bound to BOCFn3. Determined by X-ray diffraction at 1.69 Å resolution. Released 2 Jun 2010.

Method
X-ray diffraction
Resolution
1.69 Å
Organism
Homo sapiens
Chains
2
Atoms
2,476
Mol. weight
32 kDa
Ligands
CA, ZN
Released
2 Jun 2010

Explore 3N1M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3N1M contains 14 α-helices and 16 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 B: 9 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix40-434
α-helix46-483
β-strand52-5321
α-helix77-804
β-strand82-8322
β-strand89-9131
α-helix99-1013
β-strand102-10322
α-helix105-12117
β-strand127-13151
α-helix1401
α-helix144-1474
β-strand150-15561
α-helix160-1623
α-helix163-17210
β-strand177-18261
β-strand185-18951
Chain C: 5 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand717-72593
β-strand728-73473
α-helix737-7404
β-strand747-75484
α-helix760-7623
β-strand764-76964
β-strand774-77743
α-helix780-7812
β-strand785-794104
β-strand797-79824
α-helix799-8013
β-strand805-80844
α-helix809-8124

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Indian hedgehog proteinBprotein169Homo sapiensQ14623 (AlphaFold model)
Brother of CDOCprotein111Homo sapiensQ9BWV1 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>3N1M_1 Indian hedgehog protein (chains B)
GSGPGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPN
YNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESL
HYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSE
Sequence of entity 2 (C), FASTA
>3N1M_2 Brother of CDO (chains C)
GSTERPVAGPYITFTDAVNETTIMLKWMYIPASNNNTPIHGFYIYYRPTDSDNDSDYKKD
MVEGDKYWHSISHLQPETSYDIKMQCFNEGGESEFSNVMICETKARKSSGQ

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2
ZNZinc ionZn1

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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