UniProt Q91977
NMDA glutamate receptor subunit (Q91977)
NMDA glutamate receptor subunit (UniProt Q91977): 21 experimental structures on GenesisL1, 7 ligands bound, 40 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q91977
- Protein
- NMDA glutamate receptor subunit
- Experimental structures
- 21
- Predicted models
- 0
- Ligands
- 7
- Pockets
- 40 · 5 records with a druggable one
Structures
21 records of Q91977 in the MolNFT archive: 21 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 3QEK | Crystal structure of amino terminal domain of the NMDA receptor subunit GluN1 | x-ray diffraction | A, B | — | — |
| 3QEK | Crystal structure of amino terminal domain of the NMDA receptor subunit GLUN1 | x-ray diffraction | A, B | — | — |
| 3QEL | Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in… | x-ray diffraction | A, C | — | — |
| 3QEL | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | — | — |
| 3QEM | Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in… | x-ray diffraction | A, C | — | — |
| 3QEM | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | — | — |
| 5B3J | Activation of NMDA receptors and the mechanism of inhibition by ifenprodil | x-ray diffraction | A, B | — | — |
| 5B3J | Activation of NMDA receptors and the mechanism of inhibition by ifenprodil | x-ray diffraction | A, B | — | — |
| 5EWJ | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | NAG, NA, QEL | — |
| 5EWJ | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | — | — |
| 5EWL | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | NAG, NA, 5SL | 10 (best 0.77) |
| 5EWL | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | — | — |
| 5EWM | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | NAG, NA, 5SM | 9 (best 0.77) |
| 5EWM | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in… | x-ray diffraction | A, C | — | — |
| 5TPW | Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in… | x-ray diffraction | A | NAG, SO4 | 7 (best 0.75) |
| 5TPW | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2A in… | x-ray diffraction | A | NAG, SO4 | — |
| 5TPZ | Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in apo… | x-ray diffraction | A | NAG | 5 (best 0.76) |
| 5TPZ | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2B in apo… | x-ray diffraction | A | NAG | — |
| 5TQ0 | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2A in the… | x-ray diffraction | A | NAG, SO4 | — |
| 5TQ2 | Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in… | x-ray diffraction | A | ZN, NAG, SO4 | 9 (best 0.72) |
| 5TQ2 | Crystal structure of amino terminal domains of the NMDA receptor subunit GLUN1 and GLUN2A in… | x-ray diffraction | A | ZN, NAG, SO4 | — |
Ligands
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · in 10 records
- SO4 · Sulfate ion · in 5 records
- NA · Sodium ion · in 3 records
- ZN · Zinc ion · in 2 records
- 5SL · ~{N}-[(1~{S},3~{S})-3-[3-[(4-methylphenyl)methyl]-1,2,4-oxadiazol-5-yl]cyclopentyl]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-amine · in 1 record
- 5SM · 5-[3-[bis(fluoranyl)methyl]-4-fluoranyl-phenyl]-3-[(2-methylimidazol-1-yl)methyl]pyridazine · in 1 record
- QEL · 4-[(1R,2S)-2-(4-benzylpiperidin-1-yl)-1-hydroxypropyl]phenol · in 1 record
Elsewhere
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