Ligand Binding Domain of Metabotropoc glutamate receptor mGluR5 complexed with glutamate. Determined by X-ray diffraction at 2.44 Å resolution. Released 16 Feb 2010.
Explore 3LMK in 3D Show helices and sheets RCSB PDB PDBe
3LMK contains 41 α-helices and 42 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-31 | 3 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 44 | 1 | 2 |
| α-helix | 45-47 | 3 | |
| β-strand | 60 | 1 | 2 |
| α-helix | 62-66 | 5 | |
| α-helix | 67-81 | 15 | |
| α-helix | 89-90 | 2 | |
| β-strand | 91-97 | 7 | 1 |
| α-helix | 102-112 | 11 | |
| β-strand | 143-147 | 5 | 1 |
| α-helix | 152-162 | 11 | |
| α-helix | 163-165 | 3 | |
| β-strand | 169-171 | 3 | 1 |
| α-helix | 177-180 | 4 | |
| β-strand | 188-190 | 3 | 1 |
| α-helix | 195-208 | 14 | |
| β-strand | 213-219 | 7 | 3 |
| α-helix | 222-235 | 14 | |
| β-strand | 241-248 | 8 | 3 |
| α-helix | 254-267 | 14 | |
| β-strand | 273-277 | 5 | 3 |
| β-strand | 279 | 1 | 4 |
| α-helix | 280-293 | 14 | |
| β-strand | 300-303 | 4 | 3 |
| β-strand | 306 | 1 | 4 |
| α-helix | 311-314 | 4 | |
| α-helix | 318-321 | 4 | |
| β-strand | 325-329 | 5 | 3 |
| α-helix | 335-342 | 8 | |
| α-helix | 355-363 | 9 | |
| β-strand | 366 | 1 | 5 |
| α-helix | 379 | 1 | |
| β-strand | 380 | 1 | 5 |
| α-helix | 381-382 | 2 | |
| α-helix | 397-418 | 22 | |
| α-helix | 427-429 | 3 | |
| α-helix | 434-441 | 8 | |
| β-strand | 445-447 | 3 | 6 |
| α-helix | 452 | 1 | |
| β-strand | 453-455 | 3 | 6 |
| β-strand | 466-473 | 8 | 3 |
| β-strand | 479-488 | 10 | 3 |
| β-strand | 491-494 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-31 | 3 | 7 |
| β-strand | 35-41 | 7 | 7 |
| β-strand | 44 | 1 | 8 |
| α-helix | 45-48 | 4 | |
| β-strand | 60 | 1 | 8 |
| α-helix | 62-66 | 5 | |
| α-helix | 67-81 | 15 | |
| β-strand | 91-97 | 7 | 7 |
| α-helix | 102-112 | 11 | |
| β-strand | 143-147 | 5 | 7 |
| α-helix | 152-162 | 11 | |
| α-helix | 163-165 | 3 | |
| β-strand | 169-171 | 3 | 7 |
| α-helix | 177-180 | 4 | |
| β-strand | 188-190 | 3 | 7 |
| α-helix | 195-208 | 14 | |
| β-strand | 213-219 | 7 | 9 |
| α-helix | 222-237 | 16 | |
| β-strand | 241-248 | 8 | 9 |
| α-helix | 254-265 | 12 | |
| β-strand | 273-277 | 5 | 9 |
| α-helix | 280-292 | 13 | |
| β-strand | 300-303 | 4 | 9 |
| α-helix | 311-314 | 4 | |
| α-helix | 318-321 | 4 | |
| β-strand | 325-329 | 5 | 9 |
| α-helix | 332-334 | 3 | |
| α-helix | 335-341 | 7 | |
| α-helix | 355-363 | 9 | |
| β-strand | 366 | 1 | 10 |
| β-strand | 380 | 1 | 10 |
| α-helix | 397-418 | 22 | |
| α-helix | 427-429 | 3 | |
| α-helix | 434-442 | 9 | |
| β-strand | 445-447 | 3 | 11 |
| β-strand | 453-455 | 3 | 11 |
| β-strand | 466-473 | 8 | 9 |
| β-strand | 479-488 | 10 | 9 |
| β-strand | 491-494 | 4 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Metabotropic glutamate receptor 5 | A, B | protein | 492 | Homo sapiens | P41594 (AlphaFold model) |
>3LMK_1 Metabotropic glutamate receptor 5 (chains A, B) GAMDGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAML HTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGS SSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVP SDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGISIAHSYKIYSNAG EQSFDKLLKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDV TDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHRNPWFQEFWQHRFQCRLEGFPQE NSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPID GRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELK MDDDEVWSKKSN
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
| GLU | Glutamic acid | C5 H9 N O4 | 2 |
| MG | Magnesium ion | Mg | 3 |
Metabotropic Glutamate receptor mGluR5 complexed with glutamate. Dobrovetsky, E., Khutoreskaya, G., Seitova, A. et al. To be published.
Other PDB entries of the same protein (UniProt P41594 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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