9GVO: ScFv type-I interferons autoantibody pmab14

type-I interferons autoantibodies pmab15 and pmab14 in complex with Interferon alpha-2. Determined by X-ray diffraction at 1.81 Å resolution. Released 8 Oct 2025.

Method
X-ray diffraction
Resolution
1.81 Å
Organism
Homo sapiens
Chains
3
Atoms
5,172
Mol. weight
83.35 kDa
Ligands
PO4
Released
8 Oct 2025

Explore 9GVO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GVO contains 21 α-helices and 46 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.

Chain A: 5 helices, 23 β-strands

ElementResiduesLengthSheet
β-strand5-951
β-strand13-1422
β-strand20-2781
α-helix31-333
β-strand36-4163
β-strand48-5363
β-strand60-6233
β-strand70-7561
β-strand80-8561
α-helix90-923
β-strand94-10183
β-strand111-11443
β-strand118-12033
β-strand121-12222
β-strand148-15144
β-strand154-15635
β-strand163-16974
β-strand177-18265
β-strand189-19355
β-strand197-19825
α-helix1991
β-strand206-21164
β-strand214-21964
α-helix224-2263
β-strand229-23465
α-helix2401
β-strand241-24225
β-strand246-24945
Chain B: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix9-2113
α-helix26-327
α-helix40-423
α-helix53-6715
α-helix70-756
α-helix78-9720
α-helix109-13224
α-helix137-15418
Chain H: 8 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand5-956
β-strand13-1427
β-strand20-2786
α-helix31-333
β-strand36-4168
β-strand48-5368
β-strand60-6238
β-strand70-7566
α-helix76-783
β-strand80-8566
α-helix90-923
β-strand94-10188
β-strand113-11648
β-strand120-12238
β-strand123-12427
α-helix147-1493
β-strand150-15349
β-strand156-15948
β-strand165-17179
α-helix176-1783
β-strand180-18568
β-strand192-19658
β-strand200-20128
α-helix2021
β-strand209-21469
β-strand217-22269
α-helix227-2293
β-strand232-23768
α-helix243-2442
β-strand245-24628
β-strand250-25458

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
scFv type-I interferons autoantibody pmab14Aprotein290Homo sapiens
Interferon alpha-2Bprotein188Homo sapiensP01563 (AlphaFold model)
scFv type-I interferons autoantibody pmab15Hprotein294Homo sapiens
Sequence of entity 1 (A), FASTA
>9GVO_1 scFv type-I interferons autoantibody pmab14 (chains A)
RSEVQLVESGGGLVQPGGSLRLSCAASGFTFSSHAMSWVRQPPGKGLEWVSSISAAGGST
YYAASVKGRFTISRDNSNKTLYLQMNSLRAEDTAIYYCAKESDRVTTLDWFDPWGQGTLV
TVSSGTGGSGGGGSGGGGSGGGASDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWY
QQKPGQAPKLLIYAASSLQTGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYITPL
TFGGGTKVEIKGPFEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK
Sequence of entity 2 (B), FASTA
>9GVO_2 Interferon alpha-2 (chains B)
CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMI
QQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVR
KYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKEGGGGSLVPRGSGGGS
HHHHHHHH
Sequence of entity 3 (H), FASTA
>9GVO_3 scFv type-I interferons autoantibody pmab15 (chains H)
RSEVQLVESGGDLVQPGGSLRLSCAASGFTFSGYAMAWVRQAPGKEMQWVSSISDDGGTS
YYADSVEGRFTVSRDNSRSSLYLQINNLRAGDTAVYHCARDHGGNDYGDFGHFDLWGRGT
LVTVSSGTGGSGGGGSGGGGSGGGASEIVLTQSPGTLSLSPGEGATLSCRASQRVSNNYL
AWYQHRPGQAPRLLIYGASSRATGIPDRFRGSGSGTDFTLTISRLEPEDFAVYFCQQYGS
APPWTFGQGTKVEIKGPFEDDDDKAGWSHPQFEKGGGSGGGSGGGSWSHPQFEK

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P2

Water and common crystallization additives (K, GOL) are not listed.

Primary citation

Temporal and structural insights into type-I interferons autoantibodies in severe COVID-19. Vanderkerken, M., Fournier, M., Dorgham, K. et al. To be published.

Other PDB entries of the same protein (UniProt P01563 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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