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UniProt Q9Y6D9

Mitotic spindle assembly checkpoint protein MAD1 (Q9Y6D9)

Mitotic spindle assembly checkpoint protein MAD1 (UniProt Q9Y6D9): 10 experimental structures and 1 predicted model on GenesisL1, 28 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
Q9Y6D9
Protein
Mitotic spindle assembly checkpoint protein MAD1
Experimental structures
10
Predicted models
1
Pockets
28 · 2 records with a druggable one

Structures

11 records of Q9Y6D9 in the MolNFT archive: 10 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1GO4Crystal structure of Mad1-Mad2 reveals a conserved Mad2 binding motif in Mad1 and Cdc20.x-ray diffractionE, F, G, H—15 (best 0.77)
1GO4Crystal structure of MAD1-MAD2 reveals a conserved MAD2 binding motif in MAD1 and CDC20.x-ray diffractionE, F, G, H——
4DZOStructure of Human Mad1 C-terminal Domain Reveals Its Involvement in Kinetochore Targetingx-ray diffractionA, B——
4DZOStructure of human MAD1 C-terminal domain reveals its involvement in kinetochore targetingx-ray diffractionA, B——
7B1FOrthorhombic P212121 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1…x-ray diffractionB, A—2 (best 0.39)
7B1FOrthorhombic P212121 structure of human MAD1 C-terminal domain in complex with phosphorylated BUB1…x-ray diffractionB, A——
7B1HMonoclinic P21 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1 CD1…x-ray diffractionB, A, E, F—8 (best 0.69)
7B1HMonoclinic P21 structure of human MAD1 C-terminal domain in complex with phosphorylated BUB1 CD1…x-ray diffractionB, A, E, F——
7B1JOrthorhombic P21212 Structure of Human Mad1 C-terminal Domain in Complex with Phosphorylated Bub1…x-ray diffractionB, A—2 (best 0.35)
7B1JOrthorhombic P21212 structure of human MAD1 C-terminal domain in complex with phosphorylated BUB1…x-ray diffractionB, A——
Q9Y6D9AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD1 (Q9Y6D9)predictedA—1 (best 0.29)

Experiment against prediction

Elsewhere

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