Structure of Pertuzumab Fab with light chain Clambda at 2.16A. Determined by X-ray diffraction at 2.16 Å resolution. Released 29 Jan 2014.
Explore 4LLU in 3D Show helices and sheets RCSB PDB PDBe
4LLU contains 34 α-helices and 90 β-strands across 4 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 | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 57-59 | 3 | 2 |
| β-strand | 67-72 | 6 | 1 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 2 |
| β-strand | 99-103 | 7 | 2 |
| β-strand | 107-111 | 5 | 2 |
| β-strand | 117 | 1 | 3 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-127 | 8 | 4 |
| β-strand | 131 | 1 | 5 |
| β-strand | 136-145 | 10 | 4 |
| β-strand | 146 | 1 | 3 |
| β-strand | 151-154 | 4 | 6 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 6 |
| β-strand | 163-165 | 3 | 4 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 4 |
| β-strand | 176-184 | 9 | 4 |
| 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 | 10-13 | 4 | 8 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 33-38 | 6 | 8 |
| 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 |
| α-helix | 97 | 1 | |
| β-strand | 98 | 1 | 8 |
| α-helix | 99 | 1 | |
| β-strand | 102-106 | 5 | 8 |
| α-helix | 109-111 | 3 | |
| β-strand | 112 | 1 | 9 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 5 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-127 | 5 | |
| β-strand | 131-140 | 10 | 5 |
| β-strand | 141 | 1 | 9 |
| β-strand | 146-151 | 6 | 10 |
| β-strand | 154-156 | 3 | 10 |
| β-strand | 160-162 | 3 | 5 |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 5 |
| β-strand | 173-181 | 9 | 5 |
| α-helix | 183-187 | 5 | |
| β-strand | 192-198 | 7 | 10 |
| β-strand | 201-207 | 7 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 11 |
| β-strand | 10-12 | 3 | 12 |
| β-strand | 18-25 | 8 | 11 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 12 |
| β-strand | 45-51 | 7 | 12 |
| β-strand | 57-59 | 3 | 12 |
| β-strand | 68-72 | 5 | 11 |
| β-strand | 77-82 | 6 | 11 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 12 |
| β-strand | 99-103 | 7 | 12 |
| β-strand | 107-111 | 5 | 12 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 13 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 14 |
| α-helix | 128-130 | 3 | |
| β-strand | 131-132 | 2 | 14 |
| β-strand | 135-145 | 11 | 14 |
| β-strand | 146 | 1 | 13 |
| β-strand | 151-154 | 4 | 15 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 15 |
| β-strand | 163-165 | 3 | 14 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 14 |
| β-strand | 176-185 | 10 | 14 |
| β-strand | 194-200 | 7 | 15 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-211 | 7 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 16 |
| β-strand | 10-11 | 2 | 17 |
| β-strand | 19-25 | 7 | 16 |
| β-strand | 33-38 | 6 | 17 |
| β-strand | 45-49 | 5 | 17 |
| β-strand | 53-54 | 2 | 17 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 16 |
| β-strand | 70-75 | 6 | 16 |
| β-strand | 85-90 | 6 | 17 |
| α-helix | 97 | 1 | |
| β-strand | 98 | 1 | 17 |
| α-helix | 99 | 1 | |
| β-strand | 102-104 | 3 | 17 |
| β-strand | 112 | 1 | 18 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 19 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-127 | 5 | |
| β-strand | 131-140 | 10 | 19 |
| β-strand | 141 | 1 | 18 |
| β-strand | 146-151 | 6 | 20 |
| β-strand | 154-155 | 2 | 20 |
| α-helix | 156 | 1 | |
| β-strand | 160-162 | 3 | 19 |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 19 |
| β-strand | 173-181 | 9 | 19 |
| α-helix | 183-188 | 6 | |
| β-strand | 192-198 | 7 | 20 |
| β-strand | 201-207 | 7 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PERTUZUMAB FAB Heavy chain | A, C | protein | 227 | Homo sapiens | S6C4R2 (AlphaFold model) |
| Light chain CLAMBDA | B, D | protein | 212 | Homo sapiens | P0DOY2 (AlphaFold model) |
>4LLU_1 PERTUZUMAB FAB Heavy chain (chains A, C) EVQLVESGGGLVQPGGSLRLSCAASGFTFTDYTMDWVRQAPGKGLEWVADVNPNSGGSIY NQRFKGRFTLSVDRSKNTLYLQMNSLRAEDTAVYYCARNLGPSFYFDYWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
>4LLU_2 Light chain CLAMBDA (chains B, D) DIQMTQSPSSLSASVGDRVTITCKASQDVSIGVAWYQQKPGKAPKLLIYSASYRYTGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQYYIYPYTFGQGTKVEIKGQPKAAPSVTLFP PSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLS LTPEQWKSHRSYSCQVTHEGSTVEKTVAPTEC
Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface. Lewis, S.M., Wu, X., Pustilnik, A. et al. Nat Biotechnol (2014) 32:191-198. DOI 10.1038/nbt.2797 · PubMed
Other PDB entries of the same protein (UniProt S6C4R2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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