Crystal structure of FAB RG6292 in complex with CD25 ecd. Determined by X-ray diffraction at 1.83 Å resolution. Released 11 Nov 2020.
Explore 6YIO in 3D Show helices and sheets RCSB PDB PDBe
6YIO contains 22 α-helices and 61 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 | 2 | 1 | 1 |
| α-helix | 6-9 | 4 | |
| β-strand | 13-16 | 4 | 2 |
| β-strand | 20-21 | 2 | 3 |
| β-strand | 25-27 | 3 | 4 |
| β-strand | 30 | 1 | 5 |
| α-helix | 36-37 | 2 | |
| β-strand | 43-48 | 6 | 4 |
| β-strand | 53-56 | 4 | 4 |
| β-strand | 99 | 1 | 4 |
| β-strand | 103-104 | 2 | 3 |
| α-helix | 105-109 | 5 | |
| β-strand | 113 | 1 | 5 |
| β-strand | 119-120 | 2 | 4 |
| β-strand | 122 | 1 | 1 |
| β-strand | 126-131 | 6 | 2 |
| α-helix | 132 | 1 | |
| β-strand | 137 | 1 | 6 |
| β-strand | 144-146 | 3 | 2 |
| β-strand | 147-150 | 4 | 7 |
| β-strand | 153-156 | 4 | 7 |
| β-strand | 163 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 8 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 9 |
| β-strand | 18-25 | 8 | 8 |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 46-51 | 6 | 9 |
| β-strand | 58-60 | 3 | 9 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 8 |
| β-strand | 78-83 | 6 | 8 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 9 |
| β-strand | 109-112 | 4 | 9 |
| β-strand | 116-120 | 5 | 9 |
| β-strand | 126 | 1 | 10 |
| α-helix | 127-128 | 2 | |
| β-strand | 129-133 | 5 | 11 |
| β-strand | 144-154 | 11 | 11 |
| β-strand | 155 | 1 | 10 |
| β-strand | 160-163 | 4 | 12 |
| α-helix | 164-166 | 3 | |
| β-strand | 168 | 1 | 12 |
| β-strand | 172-174 | 3 | 11 |
| α-helix | 175-177 | 3 | |
| β-strand | 178-179 | 2 | 11 |
| β-strand | 185-194 | 10 | 11 |
| α-helix | 195-197 | 3 | |
| β-strand | 203-209 | 7 | 12 |
| α-helix | 210-212 | 3 | |
| β-strand | 214-220 | 7 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-7 | 4 | 13 |
| β-strand | 10-13 | 4 | 14 |
| β-strand | 19-25 | 7 | 13 |
| β-strand | 33-38 | 6 | 14 |
| β-strand | 45-49 | 5 | 14 |
| β-strand | 53-54 | 2 | 14 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 13 |
| β-strand | 70-75 | 6 | 13 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 14 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 14 |
| β-strand | 102-106 | 5 | 14 |
| β-strand | 111 | 1 | 15 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 145-150 | 6 | 17 |
| β-strand | 153-154 | 2 | 17 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 16 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 17 |
| β-strand | 205-210 | 6 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interleukin-2 receptor subunit alpha | B | protein | 203 | Homo sapiens | P01589 (AlphaFold model) |
| FAB fragment heavy chain | H | protein | 227 | Homo sapiens | |
| FAB frgament light chain | L | protein | 214 | Homo sapiens |
>6YIO_1 Interleukin-2 receptor subunit alpha (chains B) ELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQCQ CTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERIYH FVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKPQA SPEGRPESETSCAHHHHHHHHHH
>6YIO_2 FAB FRAGMENT HEAVY CHAIN (chains H) QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSLAISWVRQAPGQGLEWMGGIIPIFGTANY AQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARGGSVSGTLVDFDIWGQGTMVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDK
>6YIO_3 FAB FRGAMENT LIGHT CHAIN (chains L) DIQMTQSPSTLSASVGDRVTITCRASQSISSWLAWYQQKPGKAPKLLIYKASSLESGVPS RFSGSGSGTEFTLTISSLQPDDFATYYCQQYNIYPITFGGGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
CD25-T reg -depleting antibodies preserving IL-2 signaling on effector T cells enhance effector activation and antitumor immunity. Solomon, I., Amann, M., Goubier, A. et al. Nat Cancer (2020) 1:1153-1166. DOI 10.1038/s43018-020-00133-0 · PubMed
Other PDB entries of the same protein (UniProt P01589 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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