4QC4: Fibroblast growth factor 1

Crystal structure of C117S mutant of human acidic fibroblast growth factor. Determined by X-ray diffraction at 1.49 Å resolution. Released 11 Mar 2015.

Method
X-ray diffraction
Resolution
1.49 Å
Organism
Homo sapiens
Chains
2
Atoms
2,799
Mol. weight
33.88 kDa
Ligands
FLC
Released
11 Mar 2015

Explore 4QC4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QC4 contains 10 α-helices and 28 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.

Chains A and B: 5 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand12-1651
β-strand21-2551
β-strand31-3441
β-strand44-4851
β-strand53-5861
α-helix631
β-strand64-6741
β-strand73-7641
α-helix81-833
β-strand85-9061
β-strand94-9961
α-helix103-1053
β-strand10811
β-strand11112
β-strand11611
β-strand11712
α-helix118-1192
α-helix120-1223
β-strand132-13651

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Fibroblast growth factor 1A, Bprotein146Homo sapiensP05230 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4QC4_1 Fibroblast growth factor 1 (chains A, B)
HHHHHHFNLPPGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGEV
YIKSTETGQYLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKNWFVGLKKN
GSSKRGPRTHYGQKAILFLPLPVSSD

Ligands and cofactors

IDNameFormulaCopies
FLCCitrate anionC6 H5 O72

Water and common crystallization additives (IMD, NA) are not listed.

Primary citation

Mutation choice to eliminate buried free cysteines in protein therapeutics. Xia, X., Longo, L.M., Blaber, M. J Pharm Sci (2015) 104:566-576. DOI 10.1002/jps.24188 · PubMed

Other PDB entries of the same protein (UniProt P05230 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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