Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Determined by X-ray diffraction at 1.8 Å resolution. Released 31 May 1994.
Explore 1VFB in 3D Show helices and sheets RCSB PDB PDBe
1VFB 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 | 80-84 | 5 | |
| 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 |
|---|---|---|---|---|---|
| IgG1-kappa D1.3 fv (light chain) | A | protein | 107 | Mus musculus | P01635 (AlphaFold model) |
| IgG1-kappa D1.3 fv (heavy chain) | B | protein | 116 | Mus musculus | P01820 (AlphaFold model) |
| Hen egg white lysozyme | C | protein | 129 | Gallus gallus | P00698 (AlphaFold model) |
>1VFB_1 IGG1-KAPPA D1.3 FV (LIGHT CHAIN) (chains A) DIVLTQSPASLSASVGETVTITCRASGNIHNYLAWYQQKQGKSPQLLVYYTTTLADGVPS RFSGSGSGTQYSLKINSLQPEDFGSYYCQHFWSTPRTFGGGTKLEIK
>1VFB_2 IGG1-KAPPA D1.3 FV (HEAVY CHAIN) (chains B) QVQLQESGPGLVAPSQSLSITCTVSGFSLTGYGVNWVRQPPGKGLEWLGMIWGDGNTDYN SALKSRLSISKDNSKSQVFLKMNSLHTDDTARYYCARERDYRLDYWGQGTTLTVSS
>1VFB_3 HEN EGG WHITE LYSOZYME (chains C) KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINS RWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV QAWIRGCRL
Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Bhat, T.N., Bentley, G.A., Boulot, G. et al. Proc Natl Acad Sci U S A (1994) 91:1089-1093. DOI 10.1073/pnas.91.3.1089 · 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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