Crystal structure of IGF-II antibody complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Jun 2010.
Explore 3KR3 in 3D Show helices and sheets RCSB PDB PDBe
3KR3 contains 23 α-helices and 45 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 |
|---|---|---|---|
| α-helix | 10-20 | 11 | |
| β-strand | 26 | 1 | 1 |
| α-helix | 31-34 | 4 | |
| α-helix | 37-44 | 8 | |
| α-helix | 45-49 | 5 | |
| α-helix | 53-58 | 6 | |
| β-strand | 60 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 2 |
| β-strand | 10-12 | 3 | 3 |
| β-strand | 18-25 | 8 | 2 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 3 |
| β-strand | 45-51 | 7 | 3 |
| β-strand | 58-60 | 3 | 3 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 2 |
| β-strand | 78-83 | 6 | 2 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 3 |
| β-strand | 109-112 | 4 | 3 |
| β-strand | 116-120 | 5 | 3 |
| α-helix | 124-125 | 2 | |
| β-strand | 126 | 1 | 4 |
| α-helix | 127-128 | 2 | |
| β-strand | 129-133 | 5 | 5 |
| β-strand | 144-154 | 11 | 5 |
| β-strand | 155 | 1 | 4 |
| β-strand | 160-163 | 4 | 6 |
| α-helix | 164-166 | 3 | |
| β-strand | 168 | 1 | 6 |
| β-strand | 172-174 | 3 | 5 |
| α-helix | 175-177 | 3 | |
| β-strand | 178-179 | 2 | 5 |
| β-strand | 185-194 | 10 | 5 |
| β-strand | 204-209 | 6 | 6 |
| α-helix | 210-212 | 3 | |
| β-strand | 214-219 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| β-strand | 5-8 | 4 | 7 |
| β-strand | 11-15 | 5 | 8 |
| β-strand | 20-26 | 7 | 7 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 46-50 | 5 | 8 |
| β-strand | 54-55 | 2 | 8 |
| α-helix | 56 | 1 | |
| β-strand | 63-67 | 5 | 7 |
| β-strand | 72-76 | 5 | 7 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-91 | 7 | 8 |
| α-helix | 98 | 1 | |
| β-strand | 99 | 1 | 8 |
| α-helix | 100 | 1 | |
| β-strand | 103-108 | 6 | 8 |
| β-strand | 112 | 1 | 9 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 10 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-127 | 5 | |
| β-strand | 130-140 | 11 | 10 |
| β-strand | 141 | 1 | 9 |
| β-strand | 146-151 | 6 | 11 |
| β-strand | 154-155 | 2 | 11 |
| α-helix | 156 | 1 | |
| β-strand | 160-164 | 5 | 10 |
| β-strand | 174-183 | 10 | 10 |
| α-helix | 184-188 | 5 | |
| β-strand | 192-198 | 7 | 11 |
| β-strand | 206-211 | 6 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Insulin-like growth factor II | D | protein | 67 | Homo sapiens | P01344 (AlphaFold model) |
| antibody-Fab (heavy chain) | H | protein | 251 | Homo sapiens | |
| antibody-Fab (light chain) | L | protein | 215 | Homo sapiens |
>3KR3_1 Insulin-like growth factor II (chains D) AYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYC ATPAKSE
>3KR3_2 antibody-Fab (heavy chain) (chains H) EVQLLESGGGLVQPGGSLRLSCAASGFTFSNYIMWWVRQAPGKGLEWVSVISSSGGMTRY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARDNGDYVGEKGFDIWGQGTMVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCAAAHHHHHHGAAEQK LISEEDLNGAA
>3KR3_3 antibody-Fab (light chain) (chains L) QDIQMTQSPSSLSASVGDRVTITCRASQSISNYLNWYQQKPGKAPKLLIYTASTLQSGVP SRFSGSASGTDFTLTINSLQPEDFATYSCQQSYNSPWTFGQGTKVEIKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTQEDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
A human monoclonal antibody against insulin-like growth factor-II blocks the growth of human hepatocellular carcinoma cell lines in vitro and in vivo. Dransfield, D.T., Cohen, E.H., Chang, Q. et al. Mol Cancer Ther (2010) 9:1809-1819. DOI 10.1158/1535-7163.MCT-09-1134 · PubMed
Other PDB entries of the same protein (UniProt P01344 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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