5JPW: PDB entry 5JPW

Molecular basis for protein recognition specificity of the DYNLT1/Tctex1 canonical binding groove. Characterization of the interaction with activin receptor IIB. Determined by solution NMR. Released 17 Aug 2016.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 2,160
Mol. weight: 30.86 kDa
Released: 17 Aug 2016

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

Secondary structure: helices and β-sheets

5JPW contains 8 α-helices and 12 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: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	16-31	16
α-helix	40-59	20
β-strand	64-73	10	1
β-strand	77	1	1
β-strand	80-83	4	2
β-strand	93-100	8	1
β-strand	104-113	10	1
α-helix	124-125	2
β-strand	133-136	4	2

Chain B: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	146-148	3
α-helix	159-174	16
α-helix	183-202	20
β-strand	207-216	10	2
β-strand	220	1	2
β-strand	223-226	4	1
β-strand	236-243	8	2
β-strand	247-256	10	2
α-helix	267-268	2
β-strand	276-279	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dynein light chain Tctex-type 1,Cytoplasmic dynein 1 intermediate chain 2	A, B	protein	143	Homo sapiens	P63172 (AlphaFold model), Q13409 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5JPW_1 Dynein light chain Tctex-type 1,Cytoplasmic dynein 1 intermediate chain 2 (chains A, B)
GSMEDYQAAEETAFVVDEVSNIVKEAIESAIGGNAYQHSKVNQWTTNVVEQTLSQLTKLG
KPFKYIVTCVIMQKNGAGLHTASSCFWDSSTDGSCTVRWENKTMYCIVSAFGLSIGGGSG
QSGPIKLGMAKITQVDFPPREIV

Primary citation

Molecular Basis for the Protein Recognition Specificity of the Dynein Light Chain DYNLT1/Tctex1: CHARACTERIZATION OF THE INTERACTION WITH ACTIVIN RECEPTOR IIB. Merino-Gracia, J., Zamora-Carreras, H., Bruix, M. et al. J Biol Chem (2016) 291:20962-20975. DOI 10.1074/jbc.M116.736884 · PubMed

Other PDB entries of the same protein (UniProt P63172 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8RGI 2.02 Å, Structure of DYNLT1:DYNLT2B (TCTEX1:TCTEX1D2) heterodimer.
9BLY 3.5 Å, Composite structure of full-length human dynein-1 in phi-particle conformation
8J07 4.1 Å, 96nm repeat of human respiratory doublet microtubule and associated axonemal complexes
9E28 4.4 Å, Cryo-EM structure of Phi dynein tail
9E12 4.5 Å, Full-length human dynein-1 in phi comformation under Lis1 condition
9E13 4.5 Å, Full-length human dynein-1 in phi-like comformation bound to a Lis1 dimer under Lis1…
9E14 5.0 Å, Full-length human dynein-1 in phi-like comformation bound to a Lis1 dimer under…
9YNH 5.5 Å, Full-length human cytoplasmic dynein-1 in phi-like state bound to dynactin-p150glued and…
9E23 6.2 Å, Cryo-EM structure of Pre-Chi dynein tail
8PR1 8.2 Å, Cytoplasmic dynein-B heavy chain bound to IC-LC tower
9YNE 8.46 Å, Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B-ICD…
8PR0 9.4 Å, Cytoplasmic dynein-A heavy chain bound to dynactin-p150glued and IC-LC tower

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