4L1T: Transthyretin

Transthyretin in complex with (E)-3-(dimethylamino)-5-(4-hydroxy-3,5-dimethylstyryl)benzoic acid. Determined by X-ray diffraction at 1.16 Å resolution. Released 2 Oct 2013.

Method: X-ray diffraction
Resolution: 1.16 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,160
Mol. weight: 28.18 kDa
Ligands: 1WZ
Released: 2 Oct 2013

Explore 4L1T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4L1T contains 2 α-helices and 20 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: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	12-18	7	1
β-strand	23-24	2	1
β-strand	29-35	7	2
β-strand	41-48	8	2
β-strand	54-55	2	1
β-strand	67-73	7	2
α-helix	75-81	7
β-strand	88-97	10	2
β-strand	99	1	3
β-strand	101	1	3
β-strand	104-112	9	1
β-strand	115-123	9	1

Chain B: 1 helix, 9 β-strands

Element	Residues	Length	Sheet
β-strand	12-18	7	1
β-strand	23-24	2	1
β-strand	29-35	7	2
β-strand	41-48	8	2
β-strand	54-55	2	1
β-strand	67-73	7	2
α-helix	75-81	7
β-strand	88-97	10	2
β-strand	104-112	9	1
β-strand	115-123	9	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transthyretin	A, B	protein	127	Homo sapiens	P02766 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4L1T_1 Transthyretin (chains A, B)
GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTT
EEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTA
VVTNPKE

Ligands and cofactors

ID	Name	Formula	Copies
1WZ	3-(dimethylamino)-5-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzoic acid	C19 H21 N O3	2

Primary citation

Fluorogenic small molecules requiring reaction with a specific protein to create a fluorescent conjugate for biological imaging-what we know and what we need to learn. Baranczak, A., Connelly, S., Liu, Y. et al. Biopolymers (2014) 101:484-495. DOI 10.1002/bip.22407 · PubMed

Other PDB entries of the same protein (UniProt P02766 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1F86 1.1 Å, Transthyretin THR119MET protein stabilisation
8C86 1.1 Å, Crystal structure of human transthyretin in complex with 3-O-methyltolcapone analogue 2
8W45 1.1 Å, X-ray crystal structure of V30M-TTR in complex with pinostilbene
4QXV 1.12 Å, Crystal structure of human transthyretin in complex with luteolin at 1.1 a resolution
4KY2 1.13 Å, Transthyretin in complex with the fluorescent folding sensor…
4D7B 1.15 Å, Structure of human transthyretin in complex with Tolcapone
7EJQ 1.15 Å, Crystal structure of human transthyretin in complex with…
8AWI 1.15 Å, Crystal structure of Human Transthyretin at 1.15 Angstrom resolution
6TXW 1.15 Å, V30G Transthyretin structure in complex with Tolcalpone
4HIQ 1.18 Å, The Structure of V122I Mutant Transthyretin in Complex with AG10
9H7L 1.18 Å, Human Transthyretin in Complex with 4-phenyl-1H-pyrazolo[3,4-b]pyridin-3-amine
8C85 1.19 Å, Crystal structure of human transthyretin in complex with 3-O-methyltolcapone analogue 1

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