4V2B: Rat Unc5D Ig domain 1

rat Unc5D Ig domain 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 5 Nov 2014.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 1,734
Mol. weight: 36.26 kDa
Released: 5 Nov 2014

Explore 4V2B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4V2B contains 12 α-helices and 21 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: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	51-52	2
β-strand	53-56	4	1
α-helix	57-60	4
β-strand	61-63	3	2
α-helix	67-68	2
β-strand	69-76	8	1
β-strand	80-85	6	3
β-strand	88-89	2	3
α-helix	90-91	2
α-helix	92-94	3
β-strand	95-101	7	1
β-strand	104-112	9	1
α-helix	114-119	6
β-strand	127-133	7	3
β-strand	137-145	9	3
β-strand	146-148	3	2

Chain B: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	53-56	4	3
α-helix	57-60	4
β-strand	61-63	3	4
α-helix	67-68	2
β-strand	69-76	8	3
β-strand	80-85	6	5
β-strand	88-89	2	5
α-helix	90-91	2
α-helix	92-94	3
β-strand	95-101	7	3
α-helix	107	1
β-strand	108-116	9	3
α-helix	118-123	6
β-strand	131-137	7	5
β-strand	142-144	3	5
β-strand	148-149	2	5
β-strand	150-152	3	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein UNC5D	A, B	protein	161	HOMO SAPIENS	F1LW30 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4V2B_1 PROTEIN UNC5D (chains A, B)
MGTGAADRSRGARWWLPWLGLCFWAAGAEAARGADSGEVLPDSIPSAPGTLPHFIEEPED
AYIIKSNPIALRCKARPAMQIFFKCNGEWVHQNEHVSEESLDESSGLKVREVFINVTRQQ
VEDFHGPEDYWCQCVAWSHLGTSKSRKASVRIAYLRKNFEQ

Primary citation

Flrt Structure: Balancing Repulsion and Cell Adhesion in Cortical and Vascular Development. Seiradake, E., Del Toro, D., Nagel, D. et al. Neuron (2014) 84:370. DOI 10.1016/J.NEURON.2014.10.008 · PubMed

Other PDB entries of the same protein (UniProt F1LW30 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5FTT 3.4 Å, Octameric complex of Latrophilin 3 (Lec, Olf) , Unc5D (Ig, Ig2, TSP1) and FLRT2 (LRR)
4V2C 4.0 Å, mouse FLRT2 LRR domain in complex with rat Unc5D Ig1 domain
7ZA3 4.0 Å, GPC3-Unc5D octamer structure and role in cell migration
7ZA1 4.1 Å, GPC3-Unc5D octamer structure and role in cell migration
7ZA2 4.6 Å, GPC3-Unc5D octamer structure and role in cell migration
5FTU 6.01 Å, Tetrameric complex of Latrophilin 3, Unc5D and FLRT2

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