Fv mutant y(b 32)A (vh domain) of mouse monoclonal antibody D1.3 complexed with hen egg white lysozyme. Determined by X-ray diffraction at 2.1 Å resolution. Released 23 Dec 1996.
Explore 1KIP in 3D Show helices and sheets RCSB PDB PDBe
1KIP contains 12 α-helices and 32 β-strands across 3 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 | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 98 | 1 | 2 |
| β-strand | 102-106 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 3 |
| β-strand | 11-12 | 2 | 4 |
| β-strand | 18-25 | 8 | 3 |
| β-strand | 33-39 | 7 | 5 |
| β-strand | 46-51 | 6 | 5 |
| β-strand | 57-59 | 3 | 5 |
| α-helix | 64-66 | 3 | |
| β-strand | 67-72 | 6 | 3 |
| β-strand | 77-82 | 6 | 3 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-98 | 8 | 5 |
| β-strand | 103-106 | 4 | 5 |
| β-strand | 110-112 | 3 | 5 |
| β-strand | 113-114 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 6 |
| α-helix | 5-14 | 10 | |
| β-strand | 20 | 1 | 7 |
| β-strand | 23 | 1 | 7 |
| α-helix | 25-36 | 12 | |
| β-strand | 39 | 1 | 6 |
| β-strand | 43-46 | 4 | 8 |
| β-strand | 48-53 | 6 | 8 |
| β-strand | 58-59 | 2 | 8 |
| β-strand | 65 | 1 | 9 |
| β-strand | 79 | 1 | 9 |
| α-helix | 82-84 | 3 | |
| α-helix | 89-98 | 10 | |
| α-helix | 104-107 | 4 | |
| α-helix | 109-110 | 2 | |
| α-helix | 111-115 | 5 | |
| α-helix | 120-123 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monoclonal antibody D1.3 | A | protein | 107 | Mus musculus | P01635 (AlphaFold model) |
| Monoclonal antibody D1.3 | B | protein | 116 | Mus musculus | |
| Lysozyme | C | protein | 129 | Gallus gallus | P00698 (AlphaFold model) |
>1KIP_1 MONOCLONAL ANTIBODY D1.3 (chains A) DIVLTQSPASLSASVGETVTITCRASGNIHNYLAWYQQKQGKSPQLLVYYTTTLADGVPS RFSGSGSGTQYSLKINSLQPEDFGSYYCQHFWSTPRTFGGGTKLEIK
>1KIP_2 MONOCLONAL ANTIBODY D1.3 (chains B) QVQLQESGPGLVAPSQSLSITCTVSGFSLTGAGVNWVRQPPGKGLEWLGMIWGDGNTDYN SALKSRLSISKDNSKSQVFLKMNSLHTDDTARYYCARERDYRLDYWGQGTTLTVSS
>1KIP_3 LYSOZYME (chains C) KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINS RWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV QAWIRGCRL
Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme. Fields, B.A., Goldbaum, F.A., Dall'Acqua, W. et al. Biochemistry (1996) 35:15494-15503. DOI 10.1021/bi961709e · PubMed
Other PDB entries of the same protein (UniProt P01635 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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