4HQU: Human PDGF-BB

Crystal structure of human PDGF-BB in complex with a modified nucleotide aptamer (SOMAmer SL5). Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Nov 2012.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
2
Atoms
1,382
Mol. weight
20.92 kDa
Ligands
MG
Released
21 Nov 2012

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

Secondary structure: helices and β-sheets

4HQU contains 3 α-helices and 5 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: 3 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix9-113
β-strand17-2481
α-helix25-262
α-helix27-304
β-strand37-4042
β-strand43-5081
β-strand59-78202
β-strand81-100202

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Platelet-derived growth factor subunit BAprotein109Homo sapiensP01127 (AlphaFold model)
SOMAmer SL5CDNA24
Sequence of entity 1 (A), FASTA
>4HQU_1 Platelet-derived growth factor subunit B (chains A)
SLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQC
RPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVT
Sequence of entity 2 (C), FASTA
>4HQU_2 SOMAmer SL5 (chains C)
XXACXGXXACACGCGXXXAXAGCX

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

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

Primary citation

Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets. Davies, D.R., Gelinas, A.D., Zhang, C. et al. Proc Natl Acad Sci U S A (2012) 109:19971-19976. DOI 10.1073/pnas.1213933109 · PubMed

Other PDB entries of the same protein (UniProt P01127 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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