CD28 in complex with the antibody Fab fragment AI3. Determined by X-ray diffraction at 3.05 Å resolution. Released 18 Dec 2024.
Explore 8S6Z in 3D Show helices and sheets RCSB PDB PDBe
8S6Z contains 38 α-helices and 124 β-strands across 6 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 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 57-59 | 3 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 99-102 | 4 | 2 |
| β-strand | 106-110 | 5 | 2 |
| α-helix | 113-115 | 3 | |
| β-strand | 116 | 1 | 3 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 4 |
| β-strand | 130 | 1 | 4 |
| β-strand | 134-144 | 11 | 4 |
| β-strand | 145 | 1 | 3 |
| β-strand | 150-153 | 4 | 5 |
| α-helix | 154-156 | 3 | |
| β-strand | 158 | 1 | 5 |
| β-strand | 162-164 | 3 | 4 |
| α-helix | 165-167 | 3 | |
| β-strand | 168-169 | 2 | 4 |
| β-strand | 175-184 | 10 | 4 |
| α-helix | 185-190 | 6 | |
| β-strand | 193-199 | 7 | 5 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-210 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-14 | 5 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 27C | 1 | 8 |
| β-strand | 31 | 1 | 8 |
| β-strand | 33-38 | 6 | 7 |
| β-strand | 45-49 | 5 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 6 |
| β-strand | 70-75 | 6 | 6 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 7 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 7 |
| β-strand | 102-107 | 6 | 7 |
| β-strand | 111 | 1 | 9 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 10 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 10 |
| β-strand | 140 | 1 | 9 |
| β-strand | 144-150 | 7 | 11 |
| β-strand | 153-154 | 2 | 11 |
| β-strand | 159-160 | 2 | 10 |
| β-strand | 163 | 1 | 10 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 10 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 11 |
| β-strand | 205-210 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 12 |
| β-strand | 5-6 | 2 | 13 |
| β-strand | 10-13 | 4 | 14 |
| β-strand | 14 | 1 | 15 |
| β-strand | 17 | 1 | 15 |
| β-strand | 18-24 | 7 | 13 |
| β-strand | 32-39 | 8 | 14 |
| β-strand | 45-52 | 8 | 14 |
| β-strand | 58-62 | 5 | 14 |
| β-strand | 67-72 | 6 | 13 |
| β-strand | 76-82 | 7 | 13 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-100 | 11 | 14 |
| α-helix | 103-104 | 2 | |
| β-strand | 105-106 | 2 | 14 |
| β-strand | 107 | 1 | 12 |
| β-strand | 113-117 | 5 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 27 |
| β-strand | 5-6 | 2 | 28 |
| β-strand | 10-13 | 4 | 29 |
| β-strand | 14 | 1 | 30 |
| β-strand | 17 | 1 | 30 |
| β-strand | 18-24 | 7 | 28 |
| β-strand | 32-39 | 8 | 29 |
| β-strand | 45-52 | 8 | 29 |
| β-strand | 58-61 | 4 | 29 |
| β-strand | 67-72 | 6 | 28 |
| β-strand | 76-82 | 7 | 28 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-100 | 11 | 29 |
| α-helix | 103-104 | 2 | |
| β-strand | 105-106 | 2 | 29 |
| β-strand | 107 | 1 | 27 |
| β-strand | 113-117 | 5 | 29 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heavy chain Fab fragment of AI3 antibody | A, D | protein | 223 | Homo sapiens | |
| Light chain of AI3 antibody | B, E | protein | 220 | Homo sapiens | |
| T-cell-specific surface glycoprotein CD28 | C, F | protein | 134 | Homo sapiens | P10747 (AlphaFold model) |
>8S6Z_1 Heavy chain Fab fragment of AI3 antibody (chains A, D) EVQLLESGGGLVQPGGSLRLSCAASGFTFSSYAMSWVRQAPGKGLEWVSAISGSGGSTYY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKSYGAFDYWGQGTLVTVSSASTK GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYS LSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTH
>8S6Z_2 Light chain of AI3 antibody (chains B, E) DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTR ESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQNLRPPETFGQGTKVEIKRTVAAPS VFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYS LSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>8S6Z_3 T-cell-specific surface glycoprotein CD28 (chains C, F) NKILVKQSPMLVAYDNAVNLSCKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQV YSKTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPPYLDNEKSNGTIIHVKGK HLCPSPLFPGPSKP
Water and common crystallization additives (GOL, IMD) are not listed.
NI-3201 Is a Bispecific Antibody Mediating PD-L1-Dependent CD28 Co-stimulation on T Cells for Enhanced Tumor Control. Majocchi, S., Lloveras, P., Nouveau, L. et al. Cancer Immunol Res (2025) 13:365-383. DOI 10.1158/2326-6066.CIR-24-0298 · PubMed
Other PDB entries of the same protein (UniProt P10747 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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