Structural characterisation of a monoclonal antibody specific for the PRES1 region of the hepatitis B virus. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Sept 2002.
Explore 1H3P in 3D Show helices and sheets RCSB PDB PDBe
1H3P contains 13 α-helices and 48 β-strands across 2 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 | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 16-25 | 10 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 57-58 | 2 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 64 | 1 | 1 |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82C | 9 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 2 |
| α-helix | 98-100 | 3 | |
| β-strand | 102-103 | 2 | 2 |
| β-strand | 107-111 | 5 | 2 |
| β-strand | 117 | 1 | 3 |
| β-strand | 120-124 | 5 | 4 |
| β-strand | 135-138 | 4 | 5 |
| β-strand | 139-145 | 7 | 4 |
| β-strand | 146 | 1 | 3 |
| β-strand | 151-154 | 4 | 6 |
| β-strand | 164-166 | 3 | 5 |
| α-helix | 167-169 | 3 | |
| β-strand | 170-171 | 2 | 4 |
| β-strand | 176-178 | 3 | 4 |
| β-strand | 180-185 | 6 | 5 |
| β-strand | 195-200 | 6 | 6 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-14 | 5 | 8 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 27C-27D | 2 | 9 |
| β-strand | 30-31 | 2 | 9 |
| β-strand | 33-38 | 6 | 8 |
| α-helix | 43-44 | 2 | |
| β-strand | 45-49 | 5 | 8 |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-75 | 6 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 8 |
| β-strand | 97-98 | 2 | 8 |
| β-strand | 102-107 | 6 | 8 |
| β-strand | 111 | 1 | 10 |
| β-strand | 114 | 1 | 11 |
| β-strand | 117-118 | 2 | 12 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 130-139 | 10 | 12 |
| β-strand | 140 | 1 | 10 |
| β-strand | 145-150 | 6 | 13 |
| β-strand | 153-155 | 3 | 13 |
| β-strand | 159-163 | 5 | 12 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-181 | 9 | 12 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 13 |
| β-strand | 205-210 | 6 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antibody FAB fragment | H | protein | 219 | MUS MUSCULUS | Q65ZL8 (AlphaFold model) |
| Antibody FAB fragment | L | protein | 240 | MUS MUSCULUS | Q52L64 (AlphaFold model) |
>1H3P_1 ANTIBODY FAB FRAGMENT (chains H) EVQLVESGGGLVKPGGSLKLSCAASGFTFSSYAMSWVRQSPEKRLEWVAEVSSDGSYAYY PDTLTGRFTISRDNAKNTLYLEMTSLRSEDTAMYYCASFNWDVAYWGQGTLVTVSAAKTT PPSVYPLAPGSLAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSSGVHTFPAVLQSDLYT LSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRDC
>1H3P_2 ANTIBODY FAB FRAGMENT (chains L) DIVMTQSPSSLAVSVGEKVTMSCRSSQSLLNTRTRKSYLAWFQQKPGQSPKMLIYWASTR ESGVPDRFTGSGSGTDFTLTISSVQAEDLAVYYCKQSYSLYTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNECEVQLVESGGGLVKPGGSLKLS
Structural and Functional Characterisation of a Monoclonal Antibody Specific for the Pres1 Region of Hepatitis B Virus. Pizarro, J.C., Vulliez-Le-Normand, B., Riottot, M.M. et al. FEBS Lett (2001) 509:463. DOI 10.1016/S0014-5793(01)03190-8 · PubMed
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