Crystal structure of a disease-associated anti-human GM-CSF autoantibody MB007. Determined by X-ray diffraction at 1.97 Å resolution. Released 22 Aug 2012.
Explore 4EOW in 3D Show helices and sheets RCSB PDB PDBe
4EOW contains 15 α-helices and 47 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 | 3-6 | 4 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 58-60 | 3 | 2 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 2 |
| α-helix | 106-111 | 6 | |
| β-strand | 117 | 1 | 2 |
| β-strand | 121-125 | 5 | 2 |
| β-strand | 131 | 1 | 3 |
| α-helix | 132-133 | 2 | |
| β-strand | 134-141 | 8 | 4 |
| β-strand | 149-159 | 11 | 4 |
| β-strand | 160 | 1 | 3 |
| β-strand | 165-168 | 4 | 5 |
| α-helix | 169-171 | 3 | |
| β-strand | 173 | 1 | 5 |
| β-strand | 177-179 | 3 | 4 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-184 | 2 | 4 |
| β-strand | 190-199 | 10 | 4 |
| α-helix | 200-202 | 3 | |
| β-strand | 203 | 1 | 6 |
| β-strand | 206 | 1 | 6 |
| β-strand | 209-214 | 6 | 5 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-224 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 7 |
| β-strand | 9-12 | 4 | 8 |
| β-strand | 18-23 | 6 | 7 |
| β-strand | 35-39 | 5 | 8 |
| β-strand | 46-49 | 4 | 8 |
| β-strand | 50 | 1 | 9 |
| β-strand | 54 | 1 | 9 |
| α-helix | 55-56 | 2 | |
| β-strand | 63-67 | 5 | 7 |
| β-strand | 71-76 | 6 | 7 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-93 | 9 | 8 |
| β-strand | 98-101 | 4 | 8 |
| β-strand | 105-109 | 5 | 8 |
| β-strand | 115 | 1 | 10 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 11 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-130 | 5 | |
| β-strand | 134-143 | 10 | 11 |
| β-strand | 144 | 1 | 10 |
| β-strand | 149-154 | 6 | 12 |
| β-strand | 157-159 | 3 | 12 |
| β-strand | 163-165 | 3 | 11 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 11 |
| β-strand | 176-184 | 9 | 11 |
| α-helix | 186-191 | 6 | |
| β-strand | 195-201 | 7 | 12 |
| β-strand | 204-210 | 7 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MB007 human IgG1 Fab fragment heavy chain | H | protein | 228 | Homo sapiens | P01857 (AlphaFold model) |
| MB007 IgG1 Fab fragment light chain | L | protein | 216 | Homo sapiens | P0DOY2 (AlphaFold model) |
>4EOW_1 MB007 human IgG1 Fab fragment heavy chain (chains H) QVHLVQSGSELKKPGASVKVSCKASGYSFSRYGIKWVRQAPGQGLEWMGWINTRSGVPAY AQGFTGRFVFSLDTSVDTAFLEISSLKTEDTGIYYCATRPPRFYDKTEYWEDGFDVWGRG TLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTF PAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPK
>4EOW_2 MB007 IgG1 Fab fragment light chain (chains L) QSVLTQPPSASGTPGQSVNISCSGSSSNIGNSYVYWYQQLPGTAPKLLIYRNNRRPSGVP DRFSGSKSDTSASLAISGLRSEDEADYYCATWDDSLSGRLFGGGTKLTVLGQPKAAPSVT LFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASS YLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Molecular structure of human GM-CSF in complex with a disease-associated anti-human GM-CSF autoantibody and its potential biological implications. Blech, M., Seeliger, D., Kistler, B. et al. Biochem J (2012) 447:205-215. DOI 10.1042/BJ20120884 · PubMed
Other PDB entries of the same protein (UniProt P01857 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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