5CMP: Human FLRT3 LRR domain

Name: PDB 5CMP: human FLRT3 LRR domain
Published: 2015-08-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: cell adhesion

human FLRT3 LRR domain. Determined by X-ray diffraction at 2.6 Å resolution. Released 12 Aug 2015.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,454
Mol. weight: 152.73 kDa
Ligands: NAG
Released: 12 Aug 2015

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

Secondary structure: helices and β-sheets

5CMP contains 31 α-helices and 108 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: 8 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	36-38	3	1
β-strand	41-43	3	1
β-strand	62-64	3	1
α-helix	72-74	3
α-helix	77-81	5
β-strand	87-89	3	1
β-strand	97	1	2
β-strand	108-110	3	1
β-strand	118	1	2
β-strand	119	1	3
α-helix	121-125	5
β-strand	132-134	3	1
β-strand	145	1	3
β-strand	158-160	3	1
β-strand	168	1	4
β-strand	179-181	3	1
β-strand	189	1	4
β-strand	190	1	5
α-helix	192-195	4
β-strand	203-205	3	1
α-helix	213-215	3
β-strand	216	1	5
β-strand	229-231	3	1
β-strand	239	1	6
β-strand	251-253	3	1
β-strand	261	1	6
β-strand	275-277	3	1
β-strand	299-301	3	1
β-strand	308	1	7
α-helix	314-322	9
β-strand	328-330	3	1
β-strand	333	1	8
β-strand	336	1	7
α-helix	338-340	3
β-strand	344	1	8
α-helix	345-347	3

Chain B: 8 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	36-38	3	9
β-strand	41-43	3	9
β-strand	62-64	3	9
α-helix	72-74	3
α-helix	77-81	5
β-strand	87-89	3	9
β-strand	97	1	10
β-strand	108-110	3	9
β-strand	118	1	10
β-strand	119	1	11
α-helix	121-125	5
β-strand	132-134	3	9
β-strand	145	1	11
β-strand	158-160	3	9
β-strand	168	1	12
β-strand	179-181	3	9
β-strand	189	1	12
β-strand	190	1	13
α-helix	192-195	4
β-strand	203-205	3	9
α-helix	213-215	3
β-strand	216	1	13
β-strand	229-231	3	9
β-strand	239	1	14
β-strand	251-253	3	9
β-strand	261	1	14
β-strand	275-277	3	9
β-strand	299-301	3	9
β-strand	307-308	2	15
α-helix	314-322	9
β-strand	328-330	3	9
β-strand	333	1	16
β-strand	334-336	3	15
α-helix	338-340	3
β-strand	344	1	16
α-helix	345-347	3

Chain C: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	36-38	3	17
β-strand	41-43	3	17
β-strand	62-64	3	17
α-helix	72-74	3
α-helix	79-81	3
β-strand	87-89	3	17
β-strand	97	1	18
β-strand	108-110	3	17
β-strand	118	1	18
β-strand	119	1	19
α-helix	121-125	5
β-strand	132-134	3	17
β-strand	145	1	19
β-strand	158-160	3	17
β-strand	179-181	3	17
β-strand	190	1	20
α-helix	192-195	4
β-strand	203-205	3	17
β-strand	216	1	20
β-strand	229-231	3	17
β-strand	239	1	21
β-strand	251-253	3	17
β-strand	261	1	21
β-strand	275-277	3	17
β-strand	299-301	3	17
β-strand	307-308	2	22
α-helix	314-321	8
β-strand	328-330	3	17
β-strand	333	1	23
β-strand	334-336	3	22
α-helix	338-340	3
β-strand	344	1	23
α-helix	345-347	3

Chain D: 8 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	36-38	3	24
β-strand	41-43	3	24
β-strand	62-64	3	24
α-helix	72-74	3
α-helix	79-81	3
β-strand	87-89	3	24
β-strand	97	1	25
β-strand	108-110	3	24
β-strand	118	1	25
β-strand	119	1	26
α-helix	121-125	5
β-strand	132-134	3	24
β-strand	145	1	26
β-strand	158-160	3	24
β-strand	179-181	3	24
β-strand	190	1	27
α-helix	192-195	4
β-strand	203-205	3	24
α-helix	213-215	3
β-strand	216	1	27
β-strand	229-231	3	24
β-strand	239	1	28
β-strand	251-253	3	24
β-strand	261	1	28
β-strand	275-277	3	24
β-strand	299-301	3	24
β-strand	308	1	29
α-helix	314-322	9
β-strand	328-330	3	24
β-strand	333	1	30
β-strand	336	1	29
α-helix	338-340	3
β-strand	344	1	30
α-helix	345-347	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Leucine-rich repeat transmembrane protein FLRT3	A, B, C, D	protein	333	Homo sapiens	Q9NZU0 (AlphaFold model)

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

>5CMP_1 Leucine-rich repeat transmembrane protein FLRT3 (chains A, B, C, D)
ADPGKSCPSVCRCDAGFIYCNDRFLTSIPTGIPEDATTLYLQNNQINNAGIPSDLKNLLK
VERIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVS
IEEGAFRDSNYLRLLFLSRNHLSTIPWGLPRTIEELRLDDNRISTISSPSLQGLTSLKRL
VLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTNLRKLYLQDNHINRVPP
NAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWLQSLP
VKVNVRGLMCQAPEKVRGMAIKDLNAELFDCKD

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion. Lu, Y.C., Nazarko, O.V., Sando, R. et al. Structure (2015) 23:1678-1691. DOI 10.1016/j.str.2015.06.024 · PubMed

Other PDB entries of the same protein (UniProt Q9NZU0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6JBU 1.85 Å, High resolution crystal structure of human FLRT3 LRR domain in complex with mouse CIRL3…
5CMN 3.6 Å, FLRT3 LRR domain in complex with LPHN3 Olfactomedin domain

Browse structure collections

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