Crystal structure of the complex between cnto888 fab and mcp-1 mutant p8a. Determined by X-ray diffraction at 2.8 Å resolution. Released 3 Oct 2012.
Explore 4DN4 in 3D Show helices and sheets RCSB PDB PDBe
4DN4 contains 19 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 |
|---|---|---|---|
| β-strand | 4-6 | 3 | 6 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-24 | 7 | 6 |
| β-strand | 33-39 | 7 | 7 |
| β-strand | 46-51 | 6 | 7 |
| α-helix | 53-55 | 3 | |
| β-strand | 58-60 | 3 | 7 |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 7 |
| β-strand | 108-109 | 2 | 7 |
| β-strand | 113-117 | 5 | 7 |
| β-strand | 123 | 1 | 8 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 9 |
| β-strand | 141-151 | 11 | 9 |
| β-strand | 152 | 1 | 8 |
| β-strand | 157-160 | 4 | 10 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 10 |
| β-strand | 169-171 | 3 | 9 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 9 |
| β-strand | 182-191 | 10 | 9 |
| α-helix | 192-194 | 3 | |
| β-strand | 201-206 | 6 | 10 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| α-helix | 18 | 1 | |
| β-strand | 19-29 | 11 | 1 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-50 | 5 | 2 |
| β-strand | 54-55 | 2 | 2 |
| β-strand | 63-76 | 14 | 1 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-91 | 7 | 2 |
| β-strand | 99-100 | 2 | 2 |
| β-strand | 104-108 | 5 | 2 |
| β-strand | 113 | 1 | 3 |
| α-helix | 114-115 | 2 | |
| β-strand | 116-120 | 5 | 4 |
| α-helix | 121-123 | 3 | |
| α-helix | 124-127 | 4 | |
| β-strand | 131-141 | 11 | 4 |
| β-strand | 142 | 1 | 3 |
| β-strand | 147-152 | 6 | 5 |
| β-strand | 155-156 | 2 | 5 |
| α-helix | 157 | 1 | |
| β-strand | 161-165 | 5 | 4 |
| α-helix | 166-169 | 4 | |
| β-strand | 175-184 | 10 | 4 |
| α-helix | 185-188 | 4 | |
| β-strand | 193-199 | 7 | 5 |
| β-strand | 207-212 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-21 | 3 | |
| α-helix | 22-24 | 3 | |
| β-strand | 25-31 | 7 | 11 |
| β-strand | 40-45 | 6 | 11 |
| β-strand | 50-53 | 4 | 11 |
| α-helix | 58-68 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CNTO888 light chain | L | protein | 216 | Homo sapiens | |
| CNTO888 heavy chain | H | protein | 228 | Homo sapiens | |
| C-C motif chemokine 2 | M | protein | 76 | HOMO SAPIENS | P13500 (AlphaFold model) |
>4DN4_1 CNTO888 LIGHT CHAIN (chains L) EIVLTQSPATLSLSPGERATLSCRASQSVSDAYLAWYQQKPGQAPRLLIYDASSRATGVP ARFSGSGSGTDFTLTISSLEPEDFAVYYCHQYIQLHSFTFGQGTKVEIKRTVAAPSVFIF PPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSST LTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>4DN4_2 CNTO888 HEAVY CHAIN (chains H) QVELVQSGAEVKKPGSSVKVSCKASGGTFSSYGISWVRQAPGQGLEWMGGIIPIFGTANY AQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARYDGIYGELDFWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCHHHHHH
>4DN4_3 C-C motif chemokine 2 (chains M) QPDAINAAVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWV QDSMDHLDKQTQTPKT
Structural basis for high selectivity of anti-CCL2 neutralizing antibody CNTO 888. Obmolova, G., Teplyakov, A., Malia, T.J. et al. Mol Immunol (2012) 51:227-233. DOI 10.1016/j.molimm.2012.03.022 · PubMed
Other PDB entries of the same protein (UniProt P13500 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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