Crystal Structure of P13 Alanine Variant of Antithrombin. Determined by X-ray diffraction at 2.62 Å resolution. Released 13 Apr 2004.
Explore 1OYH in 3D Show helices and sheets RCSB PDB PDBe
1OYH contains 30 α-helices and 43 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 |
|---|---|---|---|
| α-helix | 12-14 | 3 | |
| β-strand | 24 | 1 | 1 |
| α-helix | 25-27 | 3 | |
| 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 | 116-127 | 12 | |
| α-helix | 128-132 | 5 | |
| β-strand | 140-149 | 10 | 3 |
| β-strand | 152-154 | 3 | 4 |
| α-helix | 156-166 | 11 | |
| β-strand | 170-173 | 4 | 3 |
| α-helix | 175-193 | 19 | |
| β-strand | 213-221 | 9 | 3 |
| β-strand | 223-224 | 2 | 5 |
| β-strand | 225 | 1 | 6 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-240 | 6 | 2 |
| β-strand | 246-263 | 18 | 2 |
| α-helix | 264-266 | 3 | |
| β-strand | 267-273 | 7 | 2 |
| β-strand | 274 | 1 | 6 |
| β-strand | 279-285 | 7 | 2 |
| α-helix | 292-298 | 7 | |
| α-helix | 301-310 | 10 | |
| β-strand | 312-321 | 10 | 2 |
| β-strand | 323-330 | 8 | 3 |
| α-helix | 332-336 | 5 | |
| α-helix | 342-344 | 3 | |
| β-strand | 354-356 | 3 | 4 |
| β-strand | 366-375 | 10 | 3 |
| β-strand | 376 | 1 | 5 |
| β-strand | 379-380 | 2 | 5 |
| β-strand | 387-390 | 4 | 7 |
| β-strand | 400-403 | 4 | 2 |
| β-strand | 408-414 | 7 | 2 |
| α-helix | 415-417 | 3 | |
| β-strand | 419-426 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-67 | 24 | |
| β-strand | 76-78 | 3 | 7 |
| α-helix | 80-91 | 12 | |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| α-helix | 116-131 | 16 | |
| β-strand | 139-142 | 4 | 8 |
| β-strand | 145-149 | 5 | 8 |
| β-strand | 154 | 1 | 9 |
| α-helix | 156-165 | 10 | |
| β-strand | 169-173 | 5 | 8 |
| α-helix | 179-193 | 15 | |
| β-strand | 213-224 | 12 | 8 |
| β-strand | 225 | 1 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-240 | 6 | 7 |
| β-strand | 246-263 | 18 | 7 |
| β-strand | 267-273 | 7 | 7 |
| β-strand | 274 | 1 | 10 |
| β-strand | 279-285 | 7 | 7 |
| α-helix | 292-298 | 7 | |
| α-helix | 301-310 | 10 | |
| β-strand | 312-321 | 10 | 7 |
| β-strand | 323-330 | 8 | 8 |
| α-helix | 332-337 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 355 | 1 | 9 |
| β-strand | 364-375 | 12 | 8 |
| β-strand | 379-390 | 12 | 8 |
| β-strand | 408-414 | 7 | 7 |
| β-strand | 419-426 | 8 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antithrombin-III | I | protein | 432 | Homo sapiens | P01008 (AlphaFold model) |
| Antithrombin-III | L | protein | 432 | Homo sapiens | P01008 (AlphaFold model) |
>1OYH_1 Antithrombin-III (chains I) HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH FFFAKLNCRLYRKANKASKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD DLYVSDAFHKAFLEVNEEGSAAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI IFMGRVANPCVK
>1OYH_2 Antithrombin-III (chains L) HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH FFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD DLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI IFMGRVANPCVK
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
The influence of hinge region residue Glu-381 on antithrombin allostery and metastability. Johnson, D.J.D., Huntington, J.A. J Biol Chem (2004) 279:4913-4921. DOI 10.1074/jbc.M311644200 · 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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