9N1Z: C3d

Structure of C3d Bound to a Fragment of FHR-2. Determined by X-ray diffraction at 2.31 Å resolution. Released 10 Dec 2025.

Method
X-ray diffraction
Resolution
2.31 Å
Organism
Homo sapiens
Chains
4
Atoms
6,876
Mol. weight
96 kDa
Released
10 Dec 2025

Explore 9N1Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9N1Z contains 49 α-helices and 52 β-strands across 4 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: 18 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix994-9963
α-helix998-10036
α-helix1013-103119
α-helix1034-10374
α-helix1039-105719
β-strand106011
β-strand106611
α-helix1073-10753
α-helix1076-108914
α-helix1097-111014
β-strand111212
β-strand111812
α-helix1127-11293
α-helix1131-11344
α-helix1139-115315
α-helix1155-11584
α-helix1165-117915
α-helix1186-119712
α-helix1205-12128
β-strand121513
β-strand121913
α-helix1226-124318
α-helix1249-125911
α-helix1269-128416
Chain B: 7 helices, 20 β-strands
ElementResiduesLengthSheet
α-helix147-1482
β-strand14914
α-helix152-1543
β-strand158-16035
β-strand16814
β-strand173-17536
β-strand176-17835
α-helix1791
α-helix1821
β-strand183-18537
β-strand189-19136
β-strand192-19328
β-strand196-19728
α-helix198-2014
β-strand202-20437
β-strand207-20939
α-helix211-2177
β-strand219-221310
β-strand229-23139
β-strand236-238311
β-strand239-241310
α-helix2421
β-strand246-247212
β-strand254-256311
β-strand258113
β-strand261113
β-strand267-268212
Chain C: 16 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix1013-103119
α-helix1034-10374
α-helix1043-105715
β-strand1060114
β-strand1066114
α-helix1073-10753
α-helix1076-108914
α-helix1094-10963
α-helix1097-111014
β-strand1112115
β-strand1118115
α-helix1127-11293
α-helix1139-115315
α-helix1165-117915
α-helix1180-11823
α-helix1186-119813
α-helix1205-12128
β-strand1215116
β-strand1219116
α-helix1229-124214
α-helix1249-12579
α-helix1269-128416
Chain D: 8 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand149117
α-helix152-1543
β-strand158-160318
α-helix163-1653
β-strand168117
β-strand173-175319
β-strand176-178318
α-helix1791
α-helix1821
β-strand183-185320
β-strand189-191319
β-strand192-193221
β-strand196-197221
α-helix198-2014
β-strand202-204320
β-strand207-208222
α-helix211-2166
β-strand219-221323
β-strand230-231222
β-strand236-238324
β-strand239-241323
α-helix2421
β-strand246-247225
β-strand254-256324
α-helix2571
β-strand258126
β-strand261126
β-strand267-268225

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Complement C3dg fragmentA, Cprotein297Homo sapiensP01024 (AlphaFold model)
Complement factor H-related protein 2B, Dprotein131Homo sapiensP36980 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>9N1Z_1 Complement C3dg fragment (chains A, C)
GSRSTDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIK
KGYTQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILE
KQKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSIT
KAGDFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNV
EATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAP
Sequence of entity 2 (B, D), FASTA
>9N1Z_2 Complement factor H-related protein 2 (chains B, D)
GSTGSSAEKCGPPPPIDNGDITSFLLSVYAPGSSVEYQCQNLYQLEGNNQITCRNGQWSE
PPKCLDPCVISQEIMEKYNIKLKWTNQQKLYSRTGDIVEFVCKSGYHPTKSHSFRAMCQN
GKLVYPSCEEK

Primary citation

The C-terminal domain of Staphylococcus aureus Efb recruits FHR-2 to C3b, synergistically inhibiting the terminal complement pathway. Duan, H., Kortvely, E., Mary, J.L. et al. J Immunol (2026) 215. DOI 10.1093/jimmun/vkaf316 · PubMed

Other PDB entries of the same protein (UniProt P01024 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 9N1Z directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.