6PFO: Maltodextrin-binding protein,Calcitonin receptor

Crystal structure of N-glycosylated human calcitonin receptor extracellular domain in complex with salmon calcitonin (16-32). Determined by X-ray diffraction at 1.78 Å resolution. Released 12 Feb 2020.

Method: X-ray diffraction
Resolution: 1.78 Å
Organisms: Escherichia coli, Homo sapiens, Oncorhynchus sp.
Chains: 4
Atoms: 8,740
Mol. weight: 114.06 kDa
Ligands: NAG
Released: 12 Feb 2020

Explore 6PFO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6PFO contains 60 α-helices and 66 β-strands across 3 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: 29 helices, 34 β-strands

Element	Residues	Length	Sheet
α-helix	-335--333	3
β-strand	-328--325	4	1
α-helix	-318--304	15
β-strand	-300--297	4	1
α-helix	-292--283	10
β-strand	-276--272	5	1
α-helix	-271--269	3
α-helix	-268--263	6
β-strand	-259	1	2
α-helix	-252--249	4
β-strand	-246	1	3
α-helix	-244--239	6
β-strand	-237--236	2	4
β-strand	-233--232	2	4
β-strand	-229--224	6	1
β-strand	-221--217	5	5
β-strand	-207	1	6
α-helix	-206--204	3
α-helix	-203--195	9
β-strand	-190--188	3	5
α-helix	-181--172	10
β-strand	-165--163	3	7
β-strand	-160--158	3	7
α-helix	-149--135	15
α-helix	-125--117	9
β-strand	-113--108	6	5
α-helix	-106--104	3
α-helix	-103--97	7
β-strand	-93--90	4	5
α-helix	-89--87	3
β-strand	-86--85	2	6
β-strand	-82--81	2	6
α-helix	-78	1
β-strand	-77--76	2	8
β-strand	-75--69	7	1
β-strand	-68	1	2
α-helix	-62--56	7
α-helix	-55--51	5
α-helix	-48--41	8
β-strand	-34--33	2	1
β-strand	-31	1	3
α-helix	-30--24	7
α-helix	-20--9	12
β-strand	-7--6	2	8
α-helix	-5--4	2
α-helix	1-17	17
α-helix	22-35	14
α-helix	37-40	4
α-helix	46-61	16
α-helix	63-65	3
β-strand	71-72	2	9
β-strand	75-76	2	10
β-strand	81-82	2	10
β-strand	85-86	2	9
β-strand	90-94	5	11
α-helix	95-96	2
β-strand	107-111	5	11
β-strand	112	1	12
β-strand	118	1	12
β-strand	120-121	2	13
β-strand	126-127	2	13
β-strand	130	1	11
α-helix	132-134	3

Chain B: 30 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	-335--333	3
β-strand	-329--325	5	14
α-helix	-318--304	15
β-strand	-301--297	5	14
α-helix	-292--283	10
β-strand	-276--272	5	14
α-helix	-271--269	3
α-helix	-268--263	6
β-strand	-259	1	15
α-helix	-258--256	3
α-helix	-252--249	4
β-strand	-246	1	16
α-helix	-244--239	6
β-strand	-237--236	2	17
β-strand	-233--232	2	17
β-strand	-229--224	6	14
β-strand	-221--217	5	18
β-strand	-207	1	19
α-helix	-206--204	3
α-helix	-203--194	10
β-strand	-190--188	3	18
α-helix	-181--172	10
β-strand	-165--163	3	20
β-strand	-160--158	3	20
α-helix	-149--135	15
α-helix	-125--117	9
β-strand	-113--108	6	18
α-helix	-106--104	3
α-helix	-103--97	7
β-strand	-93--90	4	18
α-helix	-89--87	3
β-strand	-86--85	2	19
β-strand	-82--81	2	19
α-helix	-78	1
β-strand	-77--76	2	21
β-strand	-75--69	7	14
β-strand	-68	1	15
α-helix	-62--56	7
α-helix	-55--51	5
α-helix	-48--39	10
β-strand	-34--33	2	14
β-strand	-31	1	16
α-helix	-30--24	7
α-helix	-20--9	12
β-strand	-7--6	2	21
α-helix	-5--4	2
α-helix	1-17	17
α-helix	22-35	14
α-helix	37-40	4
α-helix	46-61	16
α-helix	63-65	3
β-strand	71-72	2	22
β-strand	75-76	2	23
β-strand	81-82	2	23
β-strand	85-86	2	22
β-strand	90-94	5	24
α-helix	95-96	2
β-strand	107-111	5	24
β-strand	120-121	2	25
β-strand	126-127	2	25
β-strand	130	1	24
α-helix	132-135	4

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	23-26	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltodextrin-binding protein,Calcitonin receptor	A, B	protein	484	Escherichia coli, Homo sapiens	P30988 (AlphaFold model)
Calcitonin	C, D	protein	18	Oncorhynchus sp.	Q92163 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6PFO_1 Maltodextrin-binding protein,Calcitonin receptor (chains A, B)
MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPD
IIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYN
KDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDI
KDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTS
KVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKP
LGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVD
EALKDAQTNAAAEFPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWD
DTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKHH
HHHH

Sequence of entity 2 (C, D), FASTA

>6PFO_2 Calcitonin (chains C, D)
LHKLQTYPRTNTGSGTPX

Ligands and cofactors

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

Water and common crystallization additives (SO4) are not listed.

Primary citation

Calcitonin Receptor N-Glycosylation Enhances Peptide Hormone Affinity by Controlling Receptor Dynamics. Lee, S.M., Jeong, Y., Simms, J. et al. J Mol Biol (2020) 432:1996-2014. DOI 10.1016/j.jmb.2020.01.028 · PubMed

Other PDB entries of the same protein (UniProt P30988 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8F0K 1.9 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385
8F0J 2.0 Å, Calcitonin Receptor in complex with Gs and Pramlintide analogue peptide San45
8F2B 2.0 Å, Amylin 3 Receptor in complex with Gs and Pramlintide analogue peptide San45
5II0 2.1 Å, Crystal structure of the human calcitonin receptor ectodomain in complex with a…
7TYF 2.2 Å, Human Amylin1 Receptor in complex with Gs and rat amylin peptide
8F2A 2.2 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385…
9BP3 2.2 Å, Human Amylin1 Receptor in complex with Gs and cagrilintide
9BUB 2.3 Å, Human calcitonin Receptor in complex with Gs and cagrilintide in the bypass conformation
7TZF 2.4 Å, Human Amylin3 Receptor in complex with Gs and rat amylin peptide
9AUC 2.4 Å, Human Amylin1 Receptor in Complex with Gs and human Calcitonin Gene-Related Peptide
9BUD 2.5 Å, Human calcitonin Receptor in complex with Gs and cagrilintide in the CT-like conformation
7TYX 2.55 Å, Human Amylin2 Receptor in complex with Gs and rat amylin peptide

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