9R2E: ARGX-121 Fab fragment
Structure of ARGX-121 Fab fragment in complex with the Fc fragment of IgA1. Determined by X-ray diffraction at 2.54 Å resolution. Released 14 May 2025.
- Method
- X-ray diffraction
- Resolution
- 2.54 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 10,097
- Mol. weight
- 148.42 kDa
- Ligands
- MG
- Released
- 14 May 2025
Explore 9R2E in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9R2E contains 55 α-helices and 130 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.
Chain A: 8 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-8 | 5 | 23 |
| β-strand | 12-13 | 2 | 24 |
| β-strand | 19-26 | 8 | 23 |
| α-helix | 30-32 | 3 | |
| β-strand | 35-40 | 6 | 25 |
| β-strand | 46-52 | 7 | 25 |
| β-strand | 59-61 | 3 | 25 |
| β-strand | 70-74 | 5 | 23 |
| β-strand | 79-84 | 6 | 23 |
| α-helix | 89-91 | 3 | |
| β-strand | 93-100 | 8 | 25 |
| β-strand | 106-109 | 4 | 25 |
| β-strand | 113-115 | 3 | 25 |
| β-strand | 116-117 | 2 | 24 |
| β-strand | 123 | 1 | 26 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 27 |
| α-helix | 131-133 | 3 | |
| β-strand | 141-151 | 11 | 27 |
| β-strand | 152 | 1 | 26 |
| β-strand | 157-160 | 4 | 28 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 28 |
| β-strand | 169-171 | 3 | 27 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 27 |
| β-strand | 182-191 | 10 | 27 |
| β-strand | 201-206 | 6 | 28 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 28 |
| α-helix | 218-220 | 3 | |
Chain B: 9 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 29 |
| β-strand | 5 | 1 | 30 |
| β-strand | 9-12 | 4 | 31 |
| β-strand | 18-23 | 6 | 30 |
| β-strand | 35-40 | 6 | 31 |
| α-helix | 45-46 | 2 | |
| β-strand | 47-51 | 5 | 31 |
| β-strand | 55-56 | 2 | 31 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 30 |
| β-strand | 72-77 | 6 | 30 |
| α-helix | 82-84 | 3 | |
| β-strand | 87-93 | 7 | 31 |
| β-strand | 99-101 | 3 | 31 |
| β-strand | 102 | 1 | 29 |
| β-strand | 105-109 | 5 | 31 |
| α-helix | 112-114 | 3 | |
| β-strand | 115 | 1 | 32 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 33 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-130 | 5 | |
| β-strand | 134-143 | 10 | 33 |
| β-strand | 144 | 1 | 32 |
| β-strand | 149-154 | 6 | 34 |
| β-strand | 157-159 | 3 | 34 |
| β-strand | 163-165 | 3 | 33 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 33 |
| β-strand | 176-184 | 9 | 33 |
| α-helix | 186-190 | 5 | |
| β-strand | 195-201 | 7 | 34 |
| β-strand | 204-210 | 7 | 34 |
Chain H: 8 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-8 | 5 | 1 |
| β-strand | 12-13 | 2 | 2 |
| β-strand | 19-26 | 8 | 1 |
| α-helix | 30-32 | 3 | |
| β-strand | 35-40 | 6 | 3 |
| β-strand | 46-52 | 7 | 3 |
| β-strand | 59-61 | 3 | 3 |
| β-strand | 69-74 | 6 | 1 |
| β-strand | 79-84 | 6 | 1 |
| α-helix | 89-91 | 3 | |
| β-strand | 93-100 | 8 | 3 |
| β-strand | 106-109 | 4 | 3 |
| β-strand | 113-115 | 3 | 3 |
| β-strand | 116-117 | 2 | 2 |
| β-strand | 123 | 1 | 4 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 5 |
| α-helix | 131-133 | 3 | |
| β-strand | 141-151 | 11 | 5 |
| β-strand | 152 | 1 | 4 |
| β-strand | 157-160 | 4 | 6 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 6 |
| β-strand | 169-171 | 3 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 5 |
| β-strand | 182-191 | 10 | 5 |
| α-helix | 192-194 | 3 | |
| β-strand | 201-206 | 6 | 6 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 6 |
Chain L: 8 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 7 |
| β-strand | 5 | 1 | 8 |
| β-strand | 9-12 | 4 | 9 |
| β-strand | 18-23 | 6 | 8 |
| β-strand | 35-40 | 6 | 9 |
| β-strand | 47-51 | 5 | 9 |
| β-strand | 55-56 | 2 | 9 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 8 |
| β-strand | 72-77 | 6 | 8 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 9 |
| β-strand | 99-101 | 3 | 9 |
| β-strand | 102 | 1 | 7 |
| β-strand | 105-109 | 5 | 9 |
| α-helix | 112-114 | 3 | |
| 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 | 186-190 | 5 | |
| β-strand | 195-201 | 7 | 12 |
| β-strand | 204-210 | 7 | 12 |
Chain P: 10 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 246-249 | 4 | 13 |
| α-helix | 250-252 | 3 | |
| α-helix | 253-258 | 6 | |
| β-strand | 264-268 | 5 | 13 |
| β-strand | 278-281 | 4 | 14 |
| β-strand | 290-291 | 2 | 13 |
| β-strand | 304-308 | 5 | 13 |
| α-helix | 312-317 | 6 | |
| β-strand | 321-322 | 2 | 15 |
| β-strand | 323-326 | 4 | 14 |
| β-strand | 334 | 1 | 14 |
| β-strand | 337-338 | 2 | 15 |
| β-strand | 348-352 | 5 | 16 |
| α-helix | 353-355 | 3 | |
| α-helix | 356-361 | 6 | |
| β-strand | 364-374 | 11 | 16 |
| β-strand | 380-385 | 6 | 17 |
| β-strand | 388-389 | 2 | 17 |
| α-helix | 390-391 | 2 | |
| α-helix | 392-394 | 3 | |
| β-strand | 396-397 | 2 | 16 |
| α-helix | 398-400 | 3 | |
| β-strand | 401-402 | 2 | 16 |
| α-helix | 403-404 | 2 | |
| β-strand | 411-420 | 10 | 16 |
| α-helix | 421-425 | 5 | |
| β-strand | 430-435 | 6 | 17 |
| β-strand | 443-448 | 6 | 17 |
Chain Q: 12 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 245-249 | 5 | 18 |
| α-helix | 250-252 | 3 | |
| α-helix | 253-258 | 6 | |
| β-strand | 264-269 | 6 | 18 |
| β-strand | 278-281 | 4 | 19 |
| β-strand | 290-295 | 6 | 18 |
| β-strand | 303-308 | 6 | 18 |
| α-helix | 312-317 | 6 | |
| α-helix | 319-320 | 2 | |
| β-strand | 321-322 | 2 | 20 |
| β-strand | 323-326 | 4 | 19 |
| β-strand | 334 | 1 | 19 |
| β-strand | 337-338 | 2 | 20 |
| α-helix | 346-347 | 2 | |
| β-strand | 348-352 | 5 | 21 |
| α-helix | 353-355 | 3 | |
| α-helix | 356-361 | 6 | |
| β-strand | 364-374 | 11 | 21 |
| β-strand | 380-385 | 6 | 22 |
| β-strand | 388-389 | 2 | 22 |
| α-helix | 390-391 | 2 | |
| α-helix | 392-394 | 3 | |
| β-strand | 395-397 | 3 | 21 |
| α-helix | 398-400 | 3 | |
| β-strand | 401-402 | 2 | 21 |
| α-helix | 403-404 | 2 | |
| β-strand | 411-420 | 10 | 21 |
| α-helix | 421-426 | 6 | |
| β-strand | 430-435 | 6 | 22 |
| β-strand | 443-448 | 6 | 22 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| ARGX-121 Fab fragment heavy chain | A, H | protein | 244 | Homo sapiens | |
| ARGX-121 Fab fragment light chain | B, L | protein | 235 | Homo sapiens | |
| Isoform 1 of Immunoglobulin heavy constant alpha 1 | P, Q | protein | 213 | Homo sapiens | P01876 (AlphaFold model) |
Sequence of entity 1 (A, H), FASTA
>9R2E_1 ARGX-121 Fab fragment heavy chain (chains A, H)
MGWSCIILFLVATATGVHSEVQLLESGGGLVQPGGSLRLSCAASGFTSSNYLMSWVRQAP
GKGLEWVSSIYHYGHNAYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKVDS
AYDFGSWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNS
GALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
DKTH
Sequence of entity 2 (B, L), FASTA
>9R2E_2 ARGX-121 Fab fragment light chain (chains B, L)
MGWSCIILFLVATATGVHSQSVLTQPPSVSGAPGQRVTISCAGTSSDIGGRTYVSWYQQL
PGTAPKLLIYKVTIRASGVPDRFSGSKSGTSASLAITGLQAEDEADYYCASHRSNNNIVF
GGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKA
GVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Sequence of entity 3 (P, Q), FASTA
>9R2E_3 Isoform 1 of Immunoglobulin heavy constant alpha 1 (chains P, Q)
CHPRLSLHRPALEDLLLGSEANLTCTLTGLRDASGVTFTWTPSSGKSAVQGPPERDLCGC
YSVSSVLPGCAEPWNHGKTFTCTAAYPESKTPLTATLSKSGNTFRPEVHLLPPPSEELAL
NELVTLTCLARGFSPKDVLVRWLQGSQELPREKYLTWASRQEPSQGTTTFAVTSILRVAA
EDWKKGDTFSCMVGHEALPLAFTQKTIDRLAGK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 3 |
Water and common crystallization additives (EDO, PEG) are not listed.
Primary citation
Structure of ARGX-121 Fab fragment in complex with the Fc fragment of IgA1. Voet, S., Provost, M., Deweirdt, L. et al. To be published.
Other PDB entries of the same protein (UniProt P01876 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9OFR 2.65 Å, Crystal structure of the human IGA1 fc fragment-fc-alpha receptor (CD89) complex
- 6UE7 2.9 Å, Structure of dimeric sIgA complex
- 1OW0 3.1 Å, Crystal structure of human FcaRI bound to IgA1-Fc
- 8SKV 3.1 Å, Structure of human SIgA1 in complex with Streptococcus pyogenes protein M4 (Arp4)
- 6LX3 3.15 Å, Cryo-EM structure of human secretory immunoglobulin A
- 2QEJ 3.2 Å, Crystal structure of a Staphylococcus aureus protein (SSL7) in complex with Fc of human…
- 8SKU 3.2 Å, Structure of human SIgA1 in complex with human CD89 (FcaR1)
- 6LXW 3.27 Å, Cryo-EM structure of human secretory immunoglobulin A in complex with the N-terminal…
- 9MBZ 3.3 Å, Cryo-EM structure of human FcRL4 bound to IgA-Fc/J
- 7UVL 3.56 Å, IgA1 Protease with IgA1 substrate
- 6XJA 4.0 Å, Streptococcus Pneumoniae IgA1 Protease with IgA1 substrate
- 1IGA Model of human IGA1 determined by solution scattering curve-fitting and homology modelling
Browse structure collections
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