Structure of Human Leukaemia Inhibitory Factor with Fab MSC1. Determined by X-ray diffraction at 3.1 Å resolution. Released 15 Jun 2022.
Explore 7N0A in 3D Show helices and sheets RCSB PDB PDBe
7N0A contains 19 α-helices and 52 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 | 1 |
| α-helix | 12 | 1 | |
| β-strand | 13-14 | 2 | 2 |
| β-strand | 19-21 | 3 | 1 |
| β-strand | 23-25 | 3 | 1 |
| β-strand | 30 | 1 | 3 |
| β-strand | 36 | 1 | 3 |
| β-strand | 38-43 | 6 | 4 |
| α-helix | 48-49 | 2 | |
| β-strand | 50-54 | 5 | 4 |
| β-strand | 58-59 | 2 | 4 |
| α-helix | 60 | 1 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 75-80 | 6 | 1 |
| β-strand | 89-95 | 7 | 4 |
| α-helix | 102 | 1 | |
| β-strand | 103 | 1 | 4 |
| β-strand | 105 | 1 | 1 |
| β-strand | 108-110 | 3 | 4 |
| β-strand | 112-113 | 2 | 2 |
| β-strand | 117 | 1 | 5 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 6 |
| α-helix | 125-127 | 3 | |
| β-strand | 135-145 | 11 | 6 |
| β-strand | 146 | 1 | 5 |
| β-strand | 150-153 | 4 | 7 |
| β-strand | 155 | 1 | 8 |
| β-strand | 156 | 1 | 9 |
| β-strand | 160 | 1 | 8 |
| β-strand | 165-169 | 5 | 6 |
| α-helix | 170-173 | 4 | |
| β-strand | 179-188 | 10 | 6 |
| α-helix | 189-192 | 4 | |
| β-strand | 197-198 | 2 | 9 |
| β-strand | 201-204 | 4 | 7 |
| β-strand | 211-212 | 2 | 7 |
| β-strand | 215-216 | 2 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 10-12 | 3 | 11 |
| β-strand | 17-25 | 9 | 10 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 11 |
| β-strand | 46-51 | 6 | 11 |
| β-strand | 60-62 | 3 | 11 |
| β-strand | 70-75 | 6 | 10 |
| β-strand | 80-86 | 7 | 10 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-101 | 8 | 11 |
| β-strand | 106-108 | 3 | 11 |
| β-strand | 112-116 | 5 | 11 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 12 |
| β-strand | 125-129 | 5 | 13 |
| β-strand | 140-150 | 11 | 13 |
| β-strand | 151 | 1 | 12 |
| β-strand | 155-159 | 5 | 14 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 14 |
| β-strand | 168-170 | 3 | 13 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-175 | 2 | 13 |
| β-strand | 181-190 | 10 | 13 |
| α-helix | 191-193 | 3 | |
| β-strand | 199-205 | 7 | 14 |
| β-strand | 210-216 | 7 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-48 | 27 | |
| α-helix | 67-69 | 3 | |
| α-helix | 76-104 | 29 | |
| α-helix | 109-137 | 29 | |
| α-helix | 155-178 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leukemia inhibitory factor | C | protein | 181 | Homo sapiens | P15018 (AlphaFold model) |
| MSC-1 Fab Light chain | A | protein | 220 | Homo sapiens | |
| MSC-1 Fab Heavy chain | B | protein | 224 | Homo sapiens |
>7N0A_1 Leukemia inhibitory factor (chains C) SPLPITPVNATCAIRHPCHNNLMNQIRSQLAQLNGSANALFILYYTAQGEPFPNNLDKLC GPNVTDFPPFHANGTEKAKLVELYRIVVYLGTSLGNITRDQKILNPSALSLHSKLNATAD ILRGLLSNVLCRLCSKYHVGHVDVTYGPDTSGKDVFQKKKLGCQLLGKYKQIIAVLAQAF G
>7N0A_2 MSC-1 Fab Light chain (chains A) DIVMTQTPLSSPVTLGQPASISCRSSQSLLDSDGHTYLNWLQQRPGQPPRLLIYSVSNLE SGVPDRFSGSGAGTDFTLKISRVEAEDVGVYYCMQATHAPPYTFGQGTKLEIKRTVAAPS VFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYS LSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>7N0A_3 MSC-1 Fab Heavy chain (chains B) QVQLQESGGGLVKPGGSLRLSCAASGFTFSHAWMHWVRQAPGKGLEWVGQIKAKSDDYAT YYAESVKGRFTISRDDSKNTLYLQMNSLKTEDTAVYYCTCWEWDLDFWGQGTMVTVSSAS TKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGL YSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKT
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (GOL) are not listed.
Therapeutic Targeting of LIF Overcomes Macrophage-mediated Immunosuppression of the Local Tumor Microenvironment. Hallett, R.M., Bonfill-Teixidor, E., Iurlaro, R. et al. Clin Cancer Res (2023) 29:791-804. DOI 10.1158/1078-0432.CCR-21-1888 · PubMed
Other PDB entries of the same protein (UniProt P15018 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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