I2 Fab (unbound) from CH65-CH67 Lineage. Determined by X-ray diffraction at 3.0 Å resolution. Released 21 Nov 2012.
Explore 4HK3 in 3D Show helices and sheets RCSB PDB PDBe
4HK3 contains 14 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 | 3-6 | 4 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 32-39 | 8 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 65 | 1 | 1 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-101 | 10 | 2 |
| β-strand | 115-116 | 2 | 2 |
| β-strand | 120-124 | 5 | 2 |
| α-helix | 127-129 | 3 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-137 | 5 | 4 |
| β-strand | 148-149 | 2 | 5 |
| β-strand | 152-158 | 7 | 4 |
| β-strand | 159 | 1 | 3 |
| β-strand | 166-167 | 2 | 6 |
| β-strand | 172 | 1 | 6 |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 179-181 | 3 | |
| β-strand | 182-183 | 2 | 4 |
| β-strand | 189-195 | 7 | 4 |
| β-strand | 197-198 | 2 | 5 |
| β-strand | 208-213 | 6 | 6 |
| α-helix | 214-216 | 3 | |
| β-strand | 218-223 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 7 |
| β-strand | 9-11 | 3 | 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 | 84-91 | 8 | 8 |
| β-strand | 96-99 | 4 | 8 |
| β-strand | 103-106 | 4 | 8 |
| α-helix | 110-112 | 3 | |
| β-strand | 113 | 1 | 10 |
| α-helix | 114-115 | 2 | |
| β-strand | 116-120 | 5 | 11 |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| β-strand | 133-141 | 9 | 11 |
| β-strand | 142 | 1 | 10 |
| β-strand | 147-152 | 6 | 12 |
| β-strand | 155-156 | 2 | 12 |
| β-strand | 161-163 | 3 | 11 |
| β-strand | 167-168 | 2 | 11 |
| β-strand | 174-181 | 8 | 11 |
| α-helix | 184-189 | 6 | |
| β-strand | 193-199 | 7 | 12 |
| β-strand | 202-208 | 7 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| I2 heavy chain | J | protein | 237 | Homo sapiens | |
| I2 light chain | N | protein | 214 | Homo sapiens | Q8N355 (AlphaFold model) |
>4HK3_1 I2 heavy chain (chains J) QVQLVQSGAEVKKPGASVKVSCKASGYTFTDYYIHWVRQAPGQGLEWMGWIHPNSGGTNY AQKFQGWVTMTRDTSISTAYMELSRLRSDDTAVYYCARGGLEPRSVDYYYYGMDVWGQGT TVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFP AVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKHHHHHH
>4HK3_2 I2 light chain (chains N) QSVLTQPPSVSVAPGQTARITCGGNNIGSKSVHWYQQKPGQAPVLVVYDDSDRPSGIPER FSGSNSGNTATLTISRVEAGDEADYYCQVWDSSSDHVVFGGGTKLTVLGQPKAAPSVTLF PPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYL SLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Preconfiguration of the antigen-binding site during affinity maturation of a broadly neutralizing influenza virus antibody. Schmidt, A.G., Xu, H., Khan, A.R. et al. Proc Natl Acad Sci U S A (2013) 110:264-269. DOI 10.1073/pnas.1218256109 · PubMed
Other PDB entries of the same protein (UniProt Q8N355 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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