3CH8: PDZ-Fibronectin fusion protein

The crystal structure of PDZ-Fibronectin fusion protein. Determined by X-ray diffraction at 1.9 Å resolution. Released 31 Mar 2009.

Method: X-ray diffraction
Resolution: 1.9 Å
Organisms: Homo sapiens, Synthetic construct
Chains: 2
Atoms: 1,625
Mol. weight: 21.95 kDa
Ligands: MG
Released: 31 Mar 2009

Explore 3CH8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3CH8 contains 5 α-helices and 18 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: 5 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
β-strand	6-10	5	2
β-strand	26-31	6	2
α-helix	45	1
β-strand	46-50	5	2
β-strand	53-54	2	2
α-helix	60-69	10
β-strand	73-80	8	2
β-strand	88-95	8	2
β-strand	97	1	1
α-helix	102-105	4
β-strand	108-116	9	3
β-strand	119-125	7	3
α-helix	126-127	2
β-strand	134-141	8	4
β-strand	149-154	6	4
β-strand	159-162	4	3
α-helix	165-166	2
β-strand	171-178	8	4
β-strand	183	1	4
β-strand	188-192	5	4

Chain P: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	4
β-strand	10-12	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
fusion protein PDZ-Fibronectin,Fibronectin	A	protein	195	Homo sapiens	Q96RT1 (AlphaFold model)
C-terminal octapeptide from protein ARVCF	P	protein	8	Synthetic construct

Sequence of entity 1 (A), FASTA

>3CH8_1 fusion protein PDZ-Fibronectin,Fibronectin (chains A)
GSPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIE
HGQAVSLLKTFQNTVELIIVREVGNGAKQEIRVRVEKDGGSGGVSSVPTNLEVVAATPTS
LLISWDAYRELPVSYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAHY
NYHYYSSPISINYRT

Sequence of entity 2 (P), FASTA

>3CH8_2 C-terminal octapeptide from protein ARVCF (chains P)
PQPVDSWV

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Primary citation

Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution. Huang, J., Makabe, K., Biancalana, M. et al. J Mol Biol (2009) 392:1221-1231. DOI 10.1016/j.jmb.2009.07.067 · PubMed

Other PDB entries of the same protein (UniProt Q96RT1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2H3L 1.0 Å, Crystal Structure of ERBIN PDZ
6Q0N 1.18 Å, Structure of the Erbin PDB domain in complex with a high-affinity peptide
6Q0M 1.2 Å, Structure of Erbin PDZ derivative E-14 with a high-affinity peptide
1MFG 1.25 Å, The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor
7LUL 1.65 Å, Structure of the MM2 Erbin PDZ variant in complex with a high-affinity peptide
2QBW 1.8 Å, The crystal structure of PDZ-Fibronectin fusion protein
6UBH 1.8 Å, Structure of the MM7 Erbin PDZ variant in complex with a high-affinity peptide
1MFL 1.88 Å, The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor
6Q0U 1.89 Å, Structure of the Erbin PDZ variant E-6a with a high-affinity C-terminal peptide
1N7T ERBIN PDZ domain bound to a phage-derived peptide

Browse structure collections

About this viewer

MolViewer shows 3CH8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.