6UVA: PDB entry 6UVA

CryoEM Structure of the active Adrenomedullin 2 receptor G protein complex with adrenomedullin 2 peptide. Determined by electron microscopy at 2.3 Å resolution. Released 1 Apr 2020.

Method: Electron microscopy
Resolution: 2.3 Å
Organisms: Homo sapiens, Lama glama
Chains: 7
Atoms: 9,561
Mol. weight: 185.51 kDa
Released: 1 Apr 2020

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

Secondary structure: helices and β-sheets

6UVA contains 40 α-helices and 55 β-strands across 7 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: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	17-38	22
β-strand	40-46	7	1
β-strand	207-214	8	1
β-strand	217-224	8	1
α-helix	234-238	5
β-strand	243-248	6	1
α-helix	265-277	13
β-strand	286-291	6	1
α-helix	313-315	3
α-helix	325-327	3
α-helix	332-350	19
β-strand	359-362	4	1
α-helix	372-390	19

Chain B: 3 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	8-24	17
α-helix	30-33	4
α-helix	38-39	2
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	146-151	6	5
β-strand	156-161	6	5
β-strand	165-170	6	5
β-strand	175-181	7	5
β-strand	189-192	4	6
β-strand	198-202	5	6
β-strand	208-212	5	6
β-strand	218-222	5	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	284-289	6	8
β-strand	294-298	5	8
β-strand	304-308	5	8
β-strand	315-320	6	2
β-strand	327-331	5	2
β-strand	336-339	4	2

Chain E: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	37-47	11
α-helix	54-57	4
α-helix	63-75	13
α-helix	87-98	12
α-helix	121-141	21

Chain G: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	15-22	8
α-helix	30-42	13
α-helix	53-55	3

Chain N: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	9
β-strand	17-23	7	9
α-helix	29-31	3
β-strand	34-39	6	10
β-strand	45-51	7	10
β-strand	58-60	3	10
β-strand	65	1	11
β-strand	68	1	11
β-strand	69-73	5	9
β-strand	78-84	7	9
α-helix	88-90	3
β-strand	92-97	6	10
β-strand	118	1	10
β-strand	122-124	3	10

Chain P: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	16-27	12

Chain R: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	37-51	15
β-strand	65	1	12
β-strand	69	1	13
β-strand	74	1	13
β-strand	78	1	12
β-strand	84-87	4	14
β-strand	100-103	4	14
α-helix	113	1
β-strand	114	1	15
β-strand	119	1	15
β-strand	123	1	14
α-helix	125-127	3
α-helix	131-166	36
α-helix	172-197	26
α-helix	205-207	3
α-helix	211-241	31
α-helix	245-246	2
α-helix	253-256	4
α-helix	257-261	5
α-helix	264-276	13
α-helix	281-283	3
α-helix	289-291	3
α-helix	292-320	29
α-helix	331-345	15
α-helix	347-350	4
α-helix	364-381	18
α-helix	382-386	5
α-helix	389-398	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short	A	protein	394	Homo sapiens	P63092 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	350	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)
Nanobody 35	N	protein	138	Lama glama
Receptor activity-modifying protein 3	E	protein	149	Homo sapiens	O60896 (AlphaFold model)
Protein ADM2	P	protein	48	Homo sapiens	Q7Z4H4
Calcitonin gene-related peptide type 1 receptor	R	protein	490	Homo sapiens	Q16602

Sequence of entity 1 (A), FASTA

>6UVA_1 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains A)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKNTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQAALKLFDSIWNNKWLRDTSVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCSVDTENIRRVFNDCRDIIQRMHLRQYELL

Sequence of entity 2 (B), FASTA

>6UVA_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MHHHHHHGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRT
LRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGN
YVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWD
IETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDIN
AICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYD
DFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>6UVA_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL

Sequence of entity 4 (N), FASTA

>6UVA_4 Nanobody 35 (chains N)
QVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWVRQAPGKGLEWVSDISQSGASISY
TGSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCARCPAPFTRDCFDVTSTTYAYRGQ
GTQVTVSSHHHHHHEPEA

Sequence of entity 5 (E), FASTA

>6UVA_5 Receptor activity-modifying protein 3 (chains E)
MKTIIALSYIFCLVFADYKDDDDKRAGGCNETGMLERLPLCGKAFADMMGKVDVWKWCNL
SEFIVYYESFTNCTEMEANVVGCYWPNPLAQGFITGIHRQFFSNCTVDRVHLEDPPDEVL
IPLIVIPVVLTVAMAGLVVWRSKRTDTLL

Sequence of entity 6 (P), FASTA

>6UVA_6 Protein ADM2 (chains P)
TQAQLLRVGCVLGTCQVQNLSHRLWQLMGPAGRQDSAPVDPSSPHSYX

Sequence of entity 7 (R), FASTA

>6UVA_7 Calcitonin gene-related peptide type 1 receptor (chains R)
MKTIIALSYIFCLVFADYKDDDDLEVLFQGPAELEESPEDSIQLGVTRNKIMTAQYECYQ
KIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGN
WFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLS
CQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWM
LCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHL
LYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFV
LIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSF
SNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYNPAGLEVLFQ
GPHHHHHHHH

Primary citation

Structure and Dynamics of Adrenomedullin Receptors AM1and AM2Reveal Key Mechanisms in the Control of Receptor Phenotype by Receptor Activity-Modifying Proteins. Liang, Y.L., Belousoff, M.J., Fletcher, M.M. et al. Acs Pharmacol Transl Sci (2020) 3:263-284. DOI 10.1021/acsptsci.9b00080 · PubMed

Other PDB entries of the same protein (UniProt P63092 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7BPH 1.57 Å, Crystal structure of GppNHp-bound GNAS in complex with the cyclic peptide inhibitor GN13
6AU6 1.7 Å, Crystal structure of GDP-bound human GNAS R201C mutant
8F0K 1.9 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385
7E5E 1.95 Å, Crystal structure of GDP-bound GNAS in complex with the cyclic peptide inhibitor GD20
7MBX 1.95 Å, Human Cholecystokinin 1 receptor (CCK1R) Gs complex
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
9XXT 2.0 Å, Cryo-EM structure of lysophosphatidylserine (18:0)-bound GPR174-Gs complex
6X18 2.1 Å, GLP-1 peptide hormone bound to Glucagon-Like peptide-1 (GLP-1) Receptor
6X19 2.1 Å, Non peptide agonist CHU-128, bound to Glucagon-Like peptide-1 (GLP-1) Receptor
9NTU 2.1 Å, Cryo-EM structure of BETP-GLP-1(9-36)-GLP-1R-Gs complex
7RTB 2.14 Å, Peptide-19 bound to the Glucagon-Like Peptide-1 Receptor (GLP-1R)

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