1M12: Human Saposin C

NMR solution structure of human Saposin C. Determined by solution NMR. Released 29 Jul 2003.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
653
Mol. weight
9.42 kDa
Released
29 Jul 2003

Explore 1M12 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M12 contains 5 α-helices and 0 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: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-2018
α-helix25-317
α-helix36-383
α-helix44-6219
α-helix69-746

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Saposin CAprotein84Homo sapiensP07602 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1M12_1 SAPOSIN C (chains A)
SDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILS
ILLEEVSPELVCSMLHLCSGLVPR

Primary citation

Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles. de Alba, E., Weiler, S., Tjandra, N. Biochemistry (2003) 42:14729-14740. DOI 10.1021/bi0301338 · PubMed

Other PDB entries of the same protein (UniProt P07602 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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