Catalytic antibody 28B4 FAB fragment. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Dec 1996.
Explore 1KEM in 3D Show helices and sheets RCSB PDB PDBe
1KEM 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 | 10-12 | 3 | 7 |
| β-strand | 19-25 | 7 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 8 |
| β-strand | 46-51 | 6 | 8 |
| β-strand | 60-62 | 3 | 8 |
| β-strand | 70-75 | 6 | 6 |
| β-strand | 80-85 | 6 | 6 |
| α-helix | 90-92 | 3 | |
| β-strand | 95-102 | 8 | 8 |
| β-strand | 105-109 | 5 | 8 |
| β-strand | 113-114 | 2 | 8 |
| β-strand | 115-117 | 3 | 7 |
| β-strand | 123 | 1 | 9 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 10 |
| β-strand | 141-151 | 11 | 10 |
| β-strand | 152 | 1 | 9 |
| β-strand | 157-160 | 4 | 11 |
| α-helix | 161-163 | 3 | |
| β-strand | 169-171 | 3 | 10 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-177 | 3 | 10 |
| β-strand | 180-190 | 11 | 10 |
| β-strand | 199-205 | 7 | 11 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-216 | 7 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 39-43 | 5 | 2 |
| β-strand | 50-54 | 5 | 2 |
| β-strand | 58-59 | 2 | 2 |
| α-helix | 60 | 1 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 75-81 | 7 | 1 |
| α-helix | 85-87 | 3 | |
| β-strand | 90-95 | 6 | 2 |
| α-helix | 101 | 1 | |
| β-strand | 102-103 | 2 | 2 |
| β-strand | 107-111 | 5 | 2 |
| β-strand | 116 | 1 | 3 |
| β-strand | 119-123 | 5 | 4 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 134-144 | 11 | 4 |
| β-strand | 145 | 1 | 3 |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 158-160 | 3 | 5 |
| β-strand | 164-168 | 5 | 4 |
| β-strand | 178-187 | 10 | 4 |
| α-helix | 188-191 | 4 | |
| β-strand | 196-202 | 7 | 5 |
| α-helix | 209 | 1 | |
| β-strand | 210-215 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 28B4 FAB | L | protein | 217 | Mus musculus | |
| 28B4 FAB | H | protein | 218 | Mus musculus | P01868 (AlphaFold model) |
>1KEM_1 28B4 FAB (chains L) DVLMTQTPLSLPVSLGDQASISCRFSQSIVHSNGNTYLEWYLQKSGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPRTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
>1KEM_2 28B4 FAB (chains H) EVKLVESGGGLGQPGGSLRLSCATSGFTFTDYYFNWARQPPGKALEWLGFIRNKAKGYTT EYSASVKGRFTISRDNSQGILYLQMNTLRAEDSATYYCARWGSYAMDYWGQGTSVTVSSA KTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDL YTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVP
Insights into antibody catalysis: structure of an oxygenation catalyst at 1.9-angstrom resolution. Hsieh-Wilson, L.C., Schultz, P.G., Stevens, R.C. Proc Natl Acad Sci U S A (1996) 93:5363-5367. DOI 10.1073/pnas.93.11.5363 · 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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