Crystal Structure of a Domain-Swapped Serpin Dimer. Determined by X-ray diffraction at 2.8 Å resolution. Released 21 Oct 2008.
Explore 2ZNH in 3D Show helices and sheets RCSB PDB PDBe
2ZNH contains 29 α-helices and 42 β-strands across 2 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 | 24 | 1 | 1 |
| α-helix | 46-68 | 23 | |
| β-strand | 76-78 | 3 | 2 |
| α-helix | 80-90 | 11 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| β-strand | 115 | 1 | 1 |
| α-helix | 118-130 | 13 | |
| β-strand | 139-149 | 11 | 3 |
| β-strand | 154 | 1 | 4 |
| α-helix | 156-166 | 11 | |
| β-strand | 169-173 | 5 | 3 |
| α-helix | 175-193 | 19 | |
| β-strand | 211-224 | 14 | 3 |
| β-strand | 225 | 1 | 5 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-240 | 6 | 2 |
| β-strand | 246-262 | 17 | 2 |
| α-helix | 264-266 | 3 | |
| β-strand | 268-273 | 6 | 2 |
| β-strand | 274 | 1 | 5 |
| β-strand | 279-285 | 7 | 2 |
| α-helix | 292-298 | 7 | |
| α-helix | 301-308 | 8 | |
| α-helix | 311 | 1 | |
| β-strand | 312-321 | 10 | 2 |
| β-strand | 323-330 | 8 | 3 |
| α-helix | 331-336 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 355 | 1 | 6 |
| β-strand | 363-375 | 13 | 7 |
| β-strand | 379-391 | 13 | 7 |
| β-strand | 405 | 1 | 2 |
| β-strand | 408-414 | 7 | 2 |
| β-strand | 419-426 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24-25 | 2 | 8 |
| α-helix | 46-68 | 23 | |
| β-strand | 76-78 | 3 | 9 |
| α-helix | 80-91 | 12 | |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| β-strand | 114-115 | 2 | 8 |
| α-helix | 117-130 | 14 | |
| β-strand | 139-149 | 11 | 7 |
| β-strand | 154 | 1 | 6 |
| α-helix | 156-166 | 11 | |
| β-strand | 169-173 | 5 | 7 |
| α-helix | 175-193 | 19 | |
| β-strand | 211-224 | 14 | 7 |
| β-strand | 225 | 1 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-240 | 6 | 9 |
| β-strand | 246-262 | 17 | 9 |
| α-helix | 264-266 | 3 | |
| β-strand | 268-273 | 6 | 9 |
| β-strand | 274 | 1 | 10 |
| β-strand | 279-285 | 7 | 9 |
| α-helix | 292-298 | 7 | |
| α-helix | 301-309 | 9 | |
| β-strand | 312-321 | 10 | 9 |
| β-strand | 323-330 | 8 | 7 |
| α-helix | 331-335 | 5 | |
| α-helix | 342-344 | 3 | |
| β-strand | 355 | 1 | 4 |
| β-strand | 362-375 | 14 | 3 |
| β-strand | 379-392 | 14 | 3 |
| α-helix | 396-398 | 3 | |
| β-strand | 405 | 1 | 9 |
| β-strand | 408-414 | 7 | 9 |
| β-strand | 419-426 | 8 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antithrombin-III | A, B | protein | 432 | Homo sapiens | P01008 (AlphaFold model) |
>2ZNH_1 Antithrombin-III (chains A, B) HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH FFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD DLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI IFMGRVANPCVK
Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Yamasaki, M., Li, W., Johnson, D.J. et al. Nature (2008) 455:1255-1258. DOI 10.1038/nature07394 · PubMed
Other PDB entries of the same protein (UniProt P01008 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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