Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-1. Determined by X-ray diffraction at 2.05 Å resolution. Released 5 Jun 2013.
Explore 4JZN in 3D Show helices and sheets RCSB PDB PDBe
4JZN contains 47 α-helices and 139 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-24 | 7 | 1 |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-52 | 8 | 2 |
| β-strand | 57-60 | 4 | 2 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 2 |
| β-strand | 108-109 | 2 | 2 |
| β-strand | 113-117 | 5 | 2 |
| α-helix | 121-122 | 2 | |
| β-strand | 123 | 1 | 3 |
| β-strand | 126-130 | 5 | 4 |
| β-strand | 141-151 | 11 | 4 |
| β-strand | 152 | 1 | 3 |
| β-strand | 157-160 | 4 | 5 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 5 |
| β-strand | 169-171 | 3 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 4 |
| β-strand | 182-191 | 10 | 4 |
| α-helix | 192-194 | 3 | |
| β-strand | 195 | 1 | 6 |
| β-strand | 198 | 1 | 6 |
| β-strand | 201-206 | 6 | 5 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 7 |
| β-strand | 9-12 | 4 | 8 |
| β-strand | 18-23 | 6 | 7 |
| α-helix | 27-29 | 3 | |
| β-strand | 33-37 | 5 | 8 |
| β-strand | 44-47 | 4 | 8 |
| β-strand | 48 | 1 | 9 |
| β-strand | 52 | 1 | 9 |
| β-strand | 61-66 | 6 | 7 |
| β-strand | 69-74 | 6 | 7 |
| α-helix | 79-81 | 3 | |
| β-strand | 83-91 | 9 | 8 |
| β-strand | 94-97 | 4 | 8 |
| β-strand | 101-105 | 5 | 8 |
| β-strand | 110 | 1 | 10 |
| α-helix | 111-112 | 2 | |
| β-strand | 113-117 | 5 | 11 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-124 | 4 | |
| β-strand | 128-138 | 11 | 11 |
| β-strand | 139 | 1 | 10 |
| β-strand | 144-149 | 6 | 12 |
| β-strand | 152-153 | 2 | 12 |
| α-helix | 154 | 1 | |
| β-strand | 158-162 | 5 | 11 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 11 |
| α-helix | 182-186 | 5 | |
| β-strand | 190-196 | 7 | 12 |
| β-strand | 204-209 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 13 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 14 |
| β-strand | 18-21 | 4 | 15 |
| β-strand | 22 | 1 | 13 |
| β-strand | 33-39 | 7 | 14 |
| β-strand | 46-52 | 7 | 14 |
| β-strand | 57-60 | 4 | 14 |
| β-strand | 68-70 | 3 | 15 |
| β-strand | 80-83 | 4 | 15 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 14 |
| β-strand | 108-109 | 2 | 14 |
| β-strand | 113-117 | 5 | 14 |
| α-helix | 121-122 | 2 | |
| β-strand | 123 | 1 | 16 |
| β-strand | 126-130 | 5 | 17 |
| α-helix | 131-133 | 3 | |
| β-strand | 141-151 | 11 | 17 |
| β-strand | 152 | 1 | 16 |
| β-strand | 157-160 | 4 | 18 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 18 |
| β-strand | 169-171 | 3 | 17 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 17 |
| β-strand | 182-191 | 10 | 17 |
| α-helix | 192-194 | 3 | |
| β-strand | 195 | 1 | 19 |
| β-strand | 198 | 1 | 19 |
| β-strand | 200-206 | 7 | 18 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-217 | 7 | 18 |
| α-helix | 219-221 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 26 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 27 |
| β-strand | 18-25 | 8 | 26 |
| β-strand | 32-39 | 8 | 27 |
| β-strand | 46-52 | 7 | 27 |
| β-strand | 57-60 | 4 | 27 |
| β-strand | 68-72 | 5 | 26 |
| β-strand | 78-83 | 6 | 26 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 27 |
| β-strand | 108-109 | 2 | 27 |
| β-strand | 113-117 | 5 | 27 |
| α-helix | 121-122 | 2 | |
| β-strand | 123 | 1 | 28 |
| β-strand | 126-130 | 5 | 29 |
| β-strand | 141-151 | 11 | 29 |
| β-strand | 152 | 1 | 28 |
| β-strand | 157-160 | 4 | 30 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 30 |
| β-strand | 169-171 | 3 | 29 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 29 |
| β-strand | 182-191 | 10 | 29 |
| α-helix | 192-194 | 3 | |
| β-strand | 195 | 1 | 31 |
| β-strand | 198 | 1 | 31 |
| β-strand | 201-206 | 6 | 30 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 30 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Anti-HCV E2 Fab HC84-1 heavy chain | A, C, I | protein | 261 | Homo sapiens | |
| Anti-HCV E2 Fab HC84-1 light chain | B, D, P | protein | 215 | Homo sapiens | |
| Envelope glycoprotein E2 | K | protein | 13 | Hepatitis C virus (isolate H) | P27958 (AlphaFold model) |
>4JZN_1 Anti-HCV E2 Fab HC84-1 heavy chain (chains A, C, I) QVQLVQSGAEVKKPGSSVKVSCEASGGTLSNYVITWVRQAPGQGLEWMGGFIPTFRTAMY AQGFQGRVTITADESTSIAYMELTNLRSEDTAVYYCARGPLSRGYYDYWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKAEPKSCDKLEDDDDKAGWSHPQFE KGGGSGGGSGGGSWSHPQFEK
>4JZN_2 Anti-HCV E2 Fab HC84-1 light chain (chains B, D, P) RSSYVLTQPPSVSVAPGKTARITCGGNNIGSKSVHWYQQKPGQAPVLVVYDDSDRPSGIP ERFSGSNSGNTATLTISRVEAGDEADYYCQVWDSSSVVFGGGTKLTVLRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>4JZN_3 Envelope glycoprotein E2 (chains K) NTGWLAGLFYQHK
Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape. Krey, T., Meola, A., Keck, Z.Y. et al. PLoS Pathog (2013) 9:e1003364-e1003364. DOI 10.1371/journal.ppat.1003364 · PubMed
Other PDB entries of the same protein (UniProt P27958 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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