9BKK: PDB entry 9BKK

Cholecystokinin 1 receptor (CCK1R) sterol 7M mutant, Gq chimera (mGsqi) complex. Determined by electron microscopy at 2.51 Å resolution. Released 22 May 2024.

Method: Electron microscopy
Resolution: 2.51 Å
Organism: Homo sapiens
Chains: 5
Atoms: 6,809
Mol. weight: 123.26 kDa
Released: 22 May 2024

Explore 9BKK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9BKK contains 28 α-helices and 36 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: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	19-38	20
β-strand	40-46	7	1
α-helix	53-56	4
β-strand	208-214	7	1
β-strand	217-223	7	1
α-helix	234-238	5
β-strand	243-249	7	1
α-helix	266-277	12
β-strand	286-292	7	1
α-helix	294-302	9
α-helix	308-311	4
α-helix	313-315	3
α-helix	332-351	20
β-strand	359-363	5	1
α-helix	371-390	20

Chain B: 3 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	3-25	23
α-helix	30-33	4
β-strand	47-51	5	2
β-strand	58-63	6	3
β-strand	69-74	6	3
β-strand	78-83	6	3
β-strand	88-94	7	3
β-strand	100-105	6	4
β-strand	111-116	6	4
β-strand	120-125	6	4
β-strand	134-140	7	4
β-strand	146-153	8	5
β-strand	156-161	6	5
β-strand	166-170	5	5
β-strand	175-180	6	5
α-helix	186	1
β-strand	187-192	6	6
β-strand	198-203	6	6
β-strand	207-212	6	6
β-strand	218-223	6	6
β-strand	229-234	6	7
β-strand	240-245	6	7
β-strand	250-254	5	7
β-strand	259-264	6	7
β-strand	273-278	6	8
β-strand	285-289	5	8
β-strand	294-297	4	8
β-strand	304-307	4	8
β-strand	315-320	6	2
β-strand	327-331	5	2
β-strand	336-339	4	2

Chain G: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	7-24	18
α-helix	30-43	14
α-helix	53-55	3

Chain R: 13 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	39-68	30
α-helix	75-104	30
α-helix	111-144	34
α-helix	148-151	4
α-helix	155-172	18
α-helix	175-178	4
β-strand	183-186	4	9
β-strand	192-195	4	9
α-helix	203-214	12
α-helix	215-219	5
α-helix	220-237	18
α-helix	306-347	42
α-helix	350-367	18
α-helix	368-372	5
α-helix	375-384	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas	A	protein	253	Homo sapiens	Q5JWF2 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	340	Homo sapiens	P62873 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	71	Homo sapiens	P59768 (AlphaFold model)
Cholecystokinin-8	P	protein	9	Homo sapiens	P06307 (AlphaFold model)
Cholecystokinin receptor type A	R	protein	427	Homo sapiens	P32238

Sequence of entity 1 (A), FASTA

>9BKK_1 Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas (chains A)
HHHHHHHHGCTLSAEDKAAVERSKMIDRNLREDGEKARRTLRLLLLGADNSGKSTIVKQM
RILHGGSGGSGGTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVDSS
DYNRLQEALNDFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTP
EDATPEPGEDPRVTRAKYFIRKEFVDISTASGDGRHICYPHFTCAVDTENARRIFNDCKD
IILQMNLREYNLV

Sequence of entity 2 (B), FASTA

>9BKK_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
QSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>9BKK_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL

Sequence of entity 4 (P), FASTA

>9BKK_4 Cholecystokinin-8 (chains P)
DYMGWMDFX

Sequence of entity 5 (R), FASTA

>9BKK_5 Cholecystokinin receptor type A (chains R)
DVVDSLLVNGSNITPPCELGLENETLFCLDQPRPSKEWQPAVQILLYSLIFLLSVLGNTL
VITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFM
GTSVSVSTLNLVAIALERYSAICKPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSN
LVPFTKNNNQTANMCRFLLPNDVMQQSWHTFLLLLLFFIPGVVMAVAYGLISLELYQGIK
FEASQKKSAKERKPSTTSSGKYEDSDGCYLQKTRPPRKLELRQLSTGSSSRANRIRSNSS
AANLMAKKRVIRMLIVIVVLFFLCWMPIFSANAWRAYDTASAERRLSGTPISFILLLSYT
SSCVNPIIYCFMNKRFRLGFMATFPCCPNPGPPGARGEVGEEEEGGTTGASLSRFSYSHM
SASVPPQ

Primary citation

Cholesterol-dependent dynamic changes in the conformation of the type 1 cholecystokinin receptor affect ligand binding and G protein coupling. Harikumar, K.G., Zhao, P., Cary, B.P. et al. PLoS Biol (2024) 22:e3002673-e3002673. DOI 10.1371/journal.pbio.3002673 · PubMed

Other PDB entries of the same protein (UniProt Q5JWF2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8WW2 2.79 Å, GPR3/Gs complex
8I2G 2.8 Å, FSHR-Follicle stimulating hormone-compound 716340-Gs complex
8JLQ 2.84 Å, Fenoldopam-bound hTAAR1-Gs protein complex
9DQJ 2.9 Å, CryoEM structure of Gq-coupled MRGPRD with a new agonist EP-3945
9YGZ 3.04 Å, Cryo-EM structure of active mutant human green cone opsin (E129Q) in complex with…
9WNF 3.13 Å, 5HT2AR-miniGq heterotrimer in complex with a selective agonist IHCH-2330
8ZH8 3.19 Å, Human GPR103 -Gq complex bound to QRFP26
8JHI 3.2 Å, FZD3-Gs complex
9WND 3.2 Å, 5HT2AR-miniGq heterotrimer in complex with a psychedelic psilocin
8JLP 3.23 Å, Ralmitaront(RO-6889450)-bound hTAAR1-Gs protein complex
8GY7 3.3 Å, Cryo-EM structure of ACTH-bound melanocortin-2 receptor in complex with MRAP1 and Gs…
8JHB 3.3 Å, FZD6 Gs complex

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