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UniProt P06436

Envelope glycoprotein B (P06436)

Envelope glycoprotein B (UniProt P06436): 14 experimental structures on GenesisL1, 40 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P06436
Protein
Envelope glycoprotein B
Experimental structures
14
Predicted models
0
Pockets
40 · 2 records with a druggable one

Structures

14 records of P06436 in the MolNFT archive: 14 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1RJYMhc Class I Natural Mutant H-2Kbm8 Heavy Chain Complexed With beta-2 Microglobulin and Herpes…x-ray diffractionP, Q——
1RJYMHC class I natural mutant H-2KBM8 heavy chain complexed with beta-2 microglobulin and herpes…x-ray diffractionP, Q——
1RJZMhc Class I Natural Mutant H-2Kbm8 Heavy Chain Complexed With beta-2 Microglobulin and Herpies…x-ray diffractionP, Q——
1RJZMHC class I natural mutant H-2KBM8 heavy chain complexed with beta-2 microglobulin and herpies…x-ray diffractionP, Q——
1RK0Mhc Class I H-2Kb Heavy Chain Complexed With beta-2 Microglobulin and Herpes Simplex Virus…x-ray diffractionP——
1RK0MHC class I H-2KB heavy chain complexed with beta-2 microglobulin and herpes simplex virus…x-ray diffractionP——
1RK1Mhc Class I Natural H-2Kb Heavy Chain Complexed With beta-2 Microglobulin and Herpes Simplex Virus…x-ray diffractionP——
1RK1MHC class I natural H-2KB heavy chain complexed with beta-2 microglobulin and herpes simplex virus…x-ray diffractionP——
1T0MConformational switch in polymorphic H-2K molecules containing an HSV peptidex-ray diffractionP, Q——
1T0MConformational switch in polymorphic H-2K molecules containing an HSV peptidex-ray diffractionP, Q——
1T0NConformational switch in polymorphic H-2K molecules containing an HSV peptidex-ray diffractionP, Q——
1T0NConformational switch in polymorphic H-2K molecules containing an HSV peptidex-ray diffractionP, Q——
8RGZTrimeric HSV-1F gB ectodomain in postfusion conformation with three bound HDIT101 Fab molecules.electron microscopyA, B, C—20 (best 0.86)
8RH0Trimeric HSV-1F gB ectodomain in postfusion conformation with three bound HDIT102 Fab molecules.electron microscopyA, B, C—20 (best 0.85)

Elsewhere

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