Antibody structural organization: Role of kappa - lambda chain constant domain switch in catalytic functionality. Determined by X-ray diffraction at 1.95 Å resolution. Released 5 Feb 2014.
Explore 3ZL4 in 3D Show helices and sheets RCSB PDB PDBe
3ZL4 contains 17 α-helices and 47 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 | 11-12 | 2 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 3 |
| β-strand | 47-53 | 7 | 3 |
| β-strand | 58-60 | 3 | 3 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 3 |
| β-strand | 108-109 | 2 | 3 |
| β-strand | 113-115 | 3 | 3 |
| β-strand | 116-117 | 2 | 2 |
| α-helix | 121-122 | 2 | |
| β-strand | 123 | 1 | 4 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 5 |
| β-strand | 137-138 | 2 | 5 |
| β-strand | 141-151 | 11 | 5 |
| β-strand | 152 | 1 | 4 |
| β-strand | 157-160 | 4 | 6 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 6 |
| β-strand | 170-171 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 5 |
| β-strand | 182-191 | 10 | 5 |
| α-helix | 193-196 | 4 | |
| β-strand | 201-206 | 6 | 6 |
| β-strand | 211-216 | 6 | 6 |
| α-helix | 219-221 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 7 |
| β-strand | 9-12 | 4 | 8 |
| β-strand | 18-23 | 6 | 7 |
| β-strand | 35-39 | 5 | 8 |
| β-strand | 46-49 | 4 | 8 |
| β-strand | 50 | 1 | 9 |
| β-strand | 54 | 1 | 9 |
| α-helix | 55-56 | 2 | |
| β-strand | 63-68 | 6 | 7 |
| β-strand | 71-76 | 6 | 7 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-92 | 8 | 8 |
| β-strand | 98-100 | 3 | 8 |
| β-strand | 104-108 | 5 | 8 |
| α-helix | 111-113 | 3 | |
| β-strand | 114 | 1 | 10 |
| α-helix | 115-116 | 2 | |
| β-strand | 117-121 | 5 | 11 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-129 | 5 | |
| β-strand | 133-142 | 10 | 11 |
| β-strand | 143 | 1 | 10 |
| β-strand | 148-153 | 6 | 12 |
| β-strand | 156-158 | 3 | 12 |
| β-strand | 162-164 | 3 | 11 |
| α-helix | 165-167 | 3 | |
| β-strand | 168-169 | 2 | 11 |
| β-strand | 175-183 | 9 | 11 |
| α-helix | 185-188 | 4 | |
| β-strand | 194-200 | 7 | 12 |
| β-strand | 203-209 | 7 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| A17 antibody FAB fragment heavy chain | H | protein | 255 | Homo sapiens | Q6GMX6 (AlphaFold model) |
| A17 antibody FAB fragment lambda light chain | L | protein | 247 | Homo sapiens | A2NUT2 (AlphaFold model) |
>3ZL4_1 A17 ANTIBODY FAB FRAGMENT HEAVY CHAIN (chains H) QVQLQESGPGLVKPSETLSLTCAVSGYSISSGYYWGWIRQPPGKGLEWIGSIYHSGSTYY NPSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCAGLTQSSHNDANWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCLAMDYKDHDGDYKDHDID YKDDDDKVDHHHHHH
>3ZL4_2 A17 ANTIBODY FAB FRAGMENT LAMBDA LIGHT CHAIN (chains L) QSVLTQPPSVSAAPGQKVTISCSGSSSNIGNNYVSWYQQLPGTAPKLLIYDNNKRPSGIP DRFSGSKSGTSATLGITGLQTGDEADYYCGTWDSSLNPVFGGGTKLTVLGQPKAAPSVTL FPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSY LSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECSGIDAAAAASFLEQKLISEEDLNSAV DHHHHHH
Role of Kappa>Lambda Light-Chain Constant-Domain Switch in the Structure and Functionality of A17 Reactibody. Ponomarenko, N.A., Chatziefthimiou, S.D., Kurkova, I.N. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:708. DOI 10.1107/S1399004713032446 · PubMed
Other PDB entries of the same protein (UniProt Q6GMX6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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