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UniProt P03101

Major capsid protein L1 (P03101)

Major capsid protein L1 (UniProt P03101): 11 experimental structures on GenesisL1, 78 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P03101
Protein
Major capsid protein L1
Experimental structures
11
Predicted models
0
Pockets
78 · 4 records with a druggable one

Structures

11 records of P03101 in the MolNFT archive: 11 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
5KEPHigh resolution cryo-EM maps of Human Papillomavirus 16 reveal L2 location and heparin-induced…electron microscopyA, B, C, D, E, F——
5KEPHigh resolution cryo-EM maps of human papillomavirus 16 reveal L2 location and heparin-induced…electron microscopyA, B, C, D, E, F——
5KEQHigh resolution cryo-EM maps of Human papillomavirus 16 reveal L2 location and heparin-induced…electron microscopyA, B, C, D, E, F—20 (best 0.80)
5KEQHigh resolution cryo-EM maps of human papillomavirus 16 reveal L2 location and heparin-induced…electron microscopyA, B, C, D, E, F——
6BSPHigh-Resolution Structure Analysis of Antibody V5 and U4 Conformational Epitope on Human…electron microscopyC, D, E, F, G, H—18 (best 0.90)
6BSPHigh-resolution structure analysis of antibody V5 and U4 conformational epitope on human…electron microscopyC, D, E, F, G, H——
6BT3High-Resolution Structure Analysis of Antibody V5 Conformational Epitope on Human Papillomavirus 16electron microscopyI, J, K, L, M, N—20 (best 0.84)
6BT3High-resolution structure analysis of antibody V5 conformational epitope on human papillomavirus 16electron microscopyI, J, K, L, M, N——
7CN2Subparticle refinement of human papillomavirus type 16 pesudovirus in complex with H16.001 Fabelectron microscopyA, B, C, D, E, F—20 (best 0.79)
7CN2Subparticle refinement of human papillomavirus type 16 pesudovirus in complex with H16.001 Fabelectron microscopyA, B, C, D, E, F——
7KZFHigh resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes…electron microscopyF, B, C, D, E, A——

Elsewhere

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