5NQH: Human Fe65-PTB2 homodimer

Structure of the human Fe65-PTB2 homodimer. Determined by X-ray diffraction at 2.6 Å resolution. Released 3 May 2017.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,970
Mol. weight: 62.88 kDa
Released: 3 May 2017

Explore 5NQH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NQH contains 14 α-helices and 30 β-strands across 4 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	541-552	12	1
α-helix	559-570	12
α-helix	575-577	3
β-strand	579-585	7	1
β-strand	589-594	6	1
β-strand	600-605	6	1
α-helix	606-608	3
β-strand	609-614	6	1
β-strand	620-626	7	1
β-strand	632-639	8	1
α-helix	644-655	12
α-helix	657-658	2
β-strand	659-663	5	2

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	541-553	13	2
α-helix	559-570	12
β-strand	579-585	7	2
β-strand	589-594	6	2
β-strand	600-605	6	2
α-helix	606-608	3
β-strand	609-614	6	2
β-strand	620-627	8	2
β-strand	631-639	9	2
α-helix	644-660	17

Chain C: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	541-553	13	2
α-helix	559-570	12
β-strand	579-585	7	2
β-strand	589-594	6	2
β-strand	600-605	6	2
α-helix	606-608	3
β-strand	609-614	6	2
β-strand	620-626	7	2
β-strand	632-639	8	2
α-helix	644-661	18

Chain D: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	541-553	13	3
α-helix	559-570	12
β-strand	579-585	7	3
β-strand	589-594	6	3
β-strand	600-605	6	3
α-helix	606-608	3
β-strand	609-614	6	3
β-strand	620-625	6	3
β-strand	632-639	8	3
α-helix	644-655	12
β-strand	659-663	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Amyloid beta A4 precursor protein-binding family B member 1	A, B, C, D	protein	140	Homo sapiens	O00213 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5NQH_1 Amyloid beta A4 precursor protein-binding family B member 1 (chains A, B, C, D)
APKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTIL
HQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAA
CMLRYQKCLDARSQHHHHHH

Primary citation

Fe65-PTB2 Dimerization Mimics Fe65-APP Interaction. Feilen, L.P., Haubrich, K., Strecker, P. et al. Front Mol Neurosci (2017) 10:140-140. DOI 10.3389/fnmol.2017.00140 · PubMed

Other PDB entries of the same protein (UniProt O00213 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2HO2 1.33 Å, Structure of human FE65-WW domain in complex with hMena peptide.
2OEI 1.35 Å, Crystal structure of human FE65-WW domain in complex with human Mena peptide
3DXE 2.0 Å, Crystal structure of the intracellular domain of human APP (T668A mutant) in complex…
3DXC 2.1 Å, Crystal structure of the intracellular domain of human APP in complex with Fe65-PTB2
3D8D 2.2 Å, Crystal structure of the human Fe65-PTB1 domain
3DXD 2.2 Å, Crystal structure of the intracellular domain of human APP (T668E mutant) in complex…
2IDH 2.28 Å, Crystal Structure of human FE65 WW domain
3D8F 2.7 Å, Crystal structure of the human Fe65-PTB1 domain with bound phosphate (trigonal crystal…
3D8E 2.8 Å, Crystal structure of the human Fe65-PTB1 domain (trigonal crystal form)
2E45 Solution structure of Fe65 WW domain

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