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UniProt P16452

Protein 4.2 (P16452)

Protein 4.2 (UniProt P16452): 18 experimental structures and 1 predicted model on GenesisL1, 2 ligands bound, 51 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P16452
Protein
Protein 4.2
Experimental structures
18
Predicted models
1
Ligands
2
Pockets
51 · 8 records with a druggable one

Structures

19 records of P16452 in the MolNFT archive: 18 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
7TVZCryo-EM structure of human band 3-protein 4.2 complex in diagonal conformationelectron microscopyE—9 (best 0.86)
7TVZCryo-EM structure of human band 3-protein 4.2 complex in diagonal conformationelectron microscopyE——
7TW0Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformationelectron microscopyE——
7TW1Cryo-EM structure of human band 3-protein 4.2 complex (B2P2VERTICAL)electron microscopyE, F——
7TW3Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cellelectron microscopyE——
7TW5Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cellelectron microscopyE——
7TW6Cryo-EM structure of human ankyrin complex (B4P1A1) from red blood cellelectron microscopyE——
7UZSProtein 4.2 (local refinement from consensus reconstruction of ankyrin complex classes)electron microscopyX—7 (best 0.79)
7UZSProtein 4.2 (local refinement from consensus reconstruction of ankyrin complex classes)electron microscopyX——
7V0KConsensus refinement of human erythrocyte ankyrin-1 complex (Composite map)electron microscopyXCLR, PIO6 (best 0.85)
7V0QLocal refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complexelectron microscopyX—7 (best 0.78)
7V0QLocal refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complexelectron microscopyX——
8CS9Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complexelectron microscopyXPIO5 (best 0.83)
8CSLSub-tomogram averaging of erythrocyte ankyrin-1 complexelectron microscopyX—5 (best 0.75)
8CSWLocal refinement of protein 4.2 in Class 2 of erythrocyte ankyrin-1 complexelectron microscopyX—7 (best 0.78)
8CSWLocal refinement of protein 4.2 in class 2 of erythrocyte ankyrin-1 complexelectron microscopyX——
8CTEClass 2 of erythrocyte ankyrin-1 complex (Composite map)electron microscopyX—5 (best 0.84)
8CTEClass 2 of erythrocyte ankyrin-1 complex (composite MAP)electron microscopyX——
P16452AlphaFold monomer V2.0 prediction for protein 4.2 (P16452)predictedA——

Ligands

  • PIO · [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2, 3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate · in 2 records
  • CLR · Cholesterol · in 1 record

Experiment against prediction

Elsewhere

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