Crystal structure of antibody pc282. Determined by X-ray diffraction at 1.8 Å resolution. Released 11 May 2002.
Explore 1KCV in 3D Show helices and sheets RCSB PDB PDBe
1KCV contains 13 α-helices and 43 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 | 6 |
| β-strand | 11-12 | 2 | 7 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 34-40 | 7 | 8 |
| β-strand | 46-53 | 8 | 8 |
| β-strand | 58-60 | 3 | 8 |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 8 |
| β-strand | 105-106 | 2 | 8 |
| β-strand | 110-112 | 3 | 8 |
| β-strand | 113-114 | 2 | 7 |
| α-helix | 118-119 | 2 | |
| β-strand | 120 | 1 | 9 |
| β-strand | 123-127 | 5 | 10 |
| β-strand | 138-148 | 11 | 10 |
| β-strand | 149 | 1 | 9 |
| β-strand | 154-157 | 4 | 11 |
| α-helix | 158-160 | 3 | |
| β-strand | 166-168 | 3 | 10 |
| α-helix | 169-171 | 3 | |
| β-strand | 172-174 | 3 | 10 |
| β-strand | 177-187 | 11 | 10 |
| β-strand | 197-202 | 6 | 11 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| β-strand | 10-14 | 5 | 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 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-107 | 6 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 5 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PC282 immunoglobulin | L | protein | 214 | Mus musculus | P01837 (AlphaFold model) |
| PC282 immunoglobulin | H | protein | 217 | Mus musculus | P18532 (AlphaFold model) |
>1KCV_1 PC282 IMMUNOGLOBULIN (chains L) DIVMTQSPKSMGMSVGEAVTLNCKASENVGTYVSWYQQKPGQSPVLLIYGASNRYTGVPD RFTGSGSATDFTLTISSVQADDDADYYCGQSYSSPLTFGGGTKLELKRADAAPTSSIFPP SSEQLSSGGASVVCFLNSFYPKSIAVKWKVDGSKRANGTANSWTDQDSASSTYSMSSTLT LTKDKYERHNSYTCEATHKTSSSPVVKSFNRNEC
>1KCV_2 PC282 IMMUNOGLOBULIN (chains H) QVTLSQSGPGLVKPSQSLSLTCTVTSYSITSDYAWNWIRQFAGQSLEWMGYISYSGSTSY NPSLKSRISITRDTSKNQFFLQLNSVTTDDTATYYCARGGTGFPYWGTGTNVTVSAASTT APSVFPLVPGSATAAASAVTLGCLVKGYFPEPVTVAWNEGALSSGVLTVSAVLQSGLYTL SSNTTVASGTWPSASVTCLVAHPKSSTAADKKIEPKD
Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response. Nair, D.T., Singh, K., Siddiqui, Z. et al. J Immunol (2002) 168:2371-2382. PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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