4K12: Complement factor H

Structural Basis for Host Specificity of Factor H Binding by Streptococcus pneumoniae. Determined by X-ray diffraction at 1.08 Å resolution. Released 9 Apr 2014.

Method
X-ray diffraction
Resolution
1.08 Å
Organisms
Homo sapiens, Streptococcus pneumoniae
Chains
2
Atoms
1,483
Mol. weight
17.01 kDa
Released
9 Apr 2014

Explore 4K12 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K12 contains 6 α-helices and 11 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: 3 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix1-33
β-strand4-631
α-helix7-104
β-strand1112
β-strand13-1423
β-strand21-2331
β-strand27-3263
α-helix331
β-strand36-3724
β-strand44-4853
β-strand49-5025
β-strand53-5425
β-strand5912
β-strand61-6224
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-2625
α-helix32-5423
α-helix59-7820

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Complement factor HAprotein64Homo sapiensP08603 (AlphaFold model)
Choline binding protein ABprotein84Streptococcus pneumoniaeG6W2B2
Sequence of entity 1 (A), FASTA
>4K12_1 Complement factor H (chains A)
GSHMSCDIPVFMNARTKNDFTWFKLNDTLDYECHDGYESNTGSTTGSIVCGYNGWSDLPI
CYER
Sequence of entity 2 (B), FASTA
>4K12_2 Choline binding protein A (chains B)
GHMDSERDKARKEVEEYVKKIVGESYAKSTKKRHTITVALVNELNNIKNEYLNKIVESTS
ESELQILMMESRSKVDEAVSKFEK

Primary citation

Structural determinants of host specificity of complement Factor H recruitment by Streptococcus pneumoniae. Achila, D., Liu, A., Banerjee, R. et al. Biochem J (2015) 465:325-335. DOI 10.1042/BJ20141069 · PubMed

Other PDB entries of the same protein (UniProt P08603 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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