6BT5: Human mGlu8 Receptor

Human mGlu8 Receptor complexed with L-AP4. Determined by X-ray diffraction at 2.92 Å resolution. Released 7 Feb 2018.

Method: X-ray diffraction
Resolution: 2.92 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,834
Mol. weight: 107.82 kDa
Ligands: E7P, NAG
Released: 7 Feb 2018

Explore 6BT5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6BT5 contains 38 α-helices and 38 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: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	39-42	4	1
β-strand	46-52	7	1
β-strand	55	1	2
α-helix	56-58	3
β-strand	67	1	2
α-helix	69-74	6
α-helix	75-88	14
β-strand	98-104	7	1
α-helix	109-115	7
α-helix	116-118	3
β-strand	147-151	5	1
α-helix	156-166	11
β-strand	173-175	3	1
α-helix	181-184	4
β-strand	192-194	3	1
α-helix	199-213	15
β-strand	217-223	7	3
α-helix	226-241	16
β-strand	246-253	8	3
α-helix	257-258	2
α-helix	261-269	9
β-strand	277-281	5	3
α-helix	284-296	13
β-strand	304-307	4	3
α-helix	323-325	3
β-strand	329-333	5	3
α-helix	339-347	9
α-helix	359-367	9
α-helix	402-423	22
α-helix	432-434	3
α-helix	439-447	9
β-strand	450-452	3	4
β-strand	458-460	3	4
β-strand	470-479	10	3
β-strand	482-492	11	3
β-strand	494-497	4	3
α-helix	499-501	3

Chain B: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	40-42	3	5
β-strand	46-52	7	5
β-strand	55-57	3	6
α-helix	58	1
β-strand	64-67	4	6
α-helix	68	1
α-helix	69-74	6
α-helix	75-88	14
β-strand	98-104	7	5
α-helix	109-116	8
α-helix	117-119	3
β-strand	147-151	5	5
α-helix	156-166	11
β-strand	173-175	3	5
α-helix	181-184	4
β-strand	192-194	3	5
α-helix	199-213	15
β-strand	217-223	7	7
α-helix	226-241	16
β-strand	246-253	8	7
α-helix	257-258	2
α-helix	261-269	9
β-strand	277-281	5	7
α-helix	284-296	13
β-strand	304-307	4	7
β-strand	329-333	5	7
α-helix	339-346	8
α-helix	359-367	9
β-strand	390	1	8
β-strand	394	1	8
α-helix	402-423	22
α-helix	432-434	3
α-helix	439-447	9
β-strand	450-452	3	9
β-strand	458-460	3	9
β-strand	470-479	10	7
β-strand	482-492	11	7
β-strand	494-497	4	7
α-helix	499-501	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Metabotropic glutamate receptor 8	A, B	protein	479	Homo sapiens	O00222 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6BT5_1 Metabotropic glutamate receptor 8 (chains A, B)
AHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNI
TLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAAS
SVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWN
YVSTLASEGNYGESGVEAFTQISREIGGVSIAQSQKIPREPRPGEFEKIIKRLLETPNAR
AVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRA
SIDGFDRYFRSRTLANNRRNVWFAEFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSY
EQEGKVQFVIDAVYSMAYALHNMHKDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAG
TPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASE

Ligands and cofactors

ID	Name	Formula	Copies
E7P	(2S)-2-amino-4-phosphonobutanoic acid	C4 H10 N O5 P	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2

Primary citation

Determination of L-AP4-bound human mGlu8 receptor amino terminal domain structure and the molecular basis for L-AP4's group III mGlu receptor functional potency and selectivity. Schkeryantz, J.M., Chen, Q., Ho, J.D. et al. Bioorg Med Chem Lett (2018) 28:612-617. DOI 10.1016/j.bmcl.2018.01.037 · PubMed

Other PDB entries of the same protein (UniProt O00222 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BSZ 2.65 Å, Human mGlu8 Receptor complexed with glutamate
9N8Y 2.76 Å, Cryo EM Structure of Full Length mGluR8 Bound to Agonist L-AP4 and PAM VU6005649
6E5V 2.95 Å, human mGlu8 receptor amino terminal domain in complex with…
9MB9 2.97 Å, Cryo-EM structure of Gi-bound GPCR
9MBC 2.97 Å, Cryo-EM structure of agonist-bound GPCR
9N8Z 2.97 Å, Cryo EM Structure of Full Length mGluR8 Bound to Agonist L-AP4 and PAM VU6005649, class 2
9MBA 3.14 Å, Cryo-EM structure of complex of transducer-bound GPCR
9MBB 3.25 Å, Cryo-EM structure of antagonist-bound GPCR
9MBD 3.32 Å, Cryo-EM structure of Apo-GPCR
9Y1M 3.32 Å, Cryo EM Structure of Full Length mGluR8 in Complex with Beta-Arrestin-1 Bound to Agonist…
9Y1N 6.18 Å, Cryo EM Structure of Full lengthmGluR8 Bound to Agonist L-AP4 and PAM VU6005649 in…

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