Anti-carcinoembryonic antigen monoclonal antibody A5B7. Determined by X-ray diffraction at 2.1 Å resolution. Released 15 May 1997.
Explore 1CLO in 3D Show helices and sheets RCSB PDB PDBe
1CLO contains 14 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 | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 57-59 | 3 | 2 |
| β-strand | 64 | 1 | 6 |
| β-strand | 67-71 | 5 | 6 |
| β-strand | 77-82 | 6 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 100K-103 | 4 | 2 |
| β-strand | 107-111 | 5 | 2 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 7 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 8 |
| β-strand | 136-145 | 10 | 8 |
| β-strand | 146 | 1 | 7 |
| β-strand | 151-154 | 4 | 9 |
| α-helix | 155-157 | 3 | |
| β-strand | 163-165 | 3 | 8 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-171 | 3 | 8 |
| β-strand | 174-183 | 10 | 8 |
| β-strand | 194-199 | 6 | 9 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 9 |
| α-helix | 210 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 34-38 | 5 | 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 | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 144-150 | 7 | 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 | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 5 |
| β-strand | 201-210 | 10 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| A5B7 monoclonal antibody | L | protein | 213 | Mus musculus | |
| A5B7 monoclonal antibody | H | protein | 222 | Mus musculus | P01868 (AlphaFold model) |
>1CLO_1 A5B7 MONOCLONAL ANTIBODY (chains L) QTVLSQSPAILSASPGEKVTMTCRASSSVTYIHWYQQKPGSSPKSWIYATSNLASGVPAR FSGSGSGTSYSLTISRVEAEDAATYYCQHWSSKPPTFGGGTKLEIKRADAAPTVSIFPPS SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL TKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1CLO_2 A5B7 MONOCLONAL ANTIBODY (chains H) EVKLVESGGGLVQPGGSLRLSCATSGFTFTDYYMNWVRQPPGKALEWLGFIGNKANGYTT EYSASVKGRFTISRDKSQSILYLQMNTLRAEDSATYYCTRDRGLRFYFDYWGQGTTLTVS SAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQS DLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRD
VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs. Banfield, M.J., King, D.J., Mountain, A. et al. Proteins (1997) 29:161-171. DOI 10.1002/(SICI)1097-0134(199710)29:2<161::AID-PROT4>3.0.CO;2-G · PubMed
Other PDB entries of the same protein (UniProt P01868 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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