P14-fluorescein-N135Q-S380C-antithrombin-III. Determined by X-ray diffraction at 2.85 Å resolution. Released 26 May 2000.
Explore 1DZH in 3D Show helices and sheets RCSB PDB PDBe
1DZH contains 29 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 | 7-9 | 3 | |
| α-helix | 12-14 | 3 | |
| β-strand | 24 | 1 | 1 |
| α-helix | 46-69 | 24 | |
| β-strand | 76-78 | 3 | 2 |
| α-helix | 80-91 | 12 | |
| 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 | 139-149 | 11 | 3 |
| β-strand | 153-154 | 2 | 4 |
| α-helix | 156-166 | 11 | |
| β-strand | 170-173 | 4 | 3 |
| α-helix | 179-193 | 15 | |
| β-strand | 213-224 | 12 | 3 |
| β-strand | 225 | 1 | 5 |
| α-helix | 228-230 | 3 | |
| α-helix | 231-233 | 3 | |
| β-strand | 235-238 | 4 | 2 |
| β-strand | 248-262 | 15 | 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 | 301-310 | 10 | |
| β-strand | 312-321 | 10 | 2 |
| β-strand | 323-330 | 8 | 3 |
| α-helix | 332-338 | 7 | |
| β-strand | 354-355 | 2 | 4 |
| β-strand | 366-376 | 11 | 3 |
| β-strand | 379-380 | 2 | 3 |
| β-strand | 386-390 | 5 | 6 |
| β-strand | 401-403 | 3 | 2 |
| β-strand | 408-414 | 7 | 2 |
| β-strand | 419-426 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-69 | 25 | |
| β-strand | 76-78 | 3 | 6 |
| α-helix | 80-91 | 12 | |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| α-helix | 119-131 | 13 | |
| β-strand | 139-142 | 4 | 7 |
| β-strand | 145-149 | 5 | 7 |
| β-strand | 154 | 1 | 8 |
| α-helix | 156-161 | 6 | |
| α-helix | 162-166 | 5 | |
| β-strand | 169-173 | 5 | 7 |
| α-helix | 180-193 | 14 | |
| β-strand | 213-224 | 12 | 7 |
| β-strand | 225 | 1 | 9 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-241 | 7 | 10 |
| β-strand | 245-251 | 7 | 10 |
| β-strand | 254-263 | 10 | 6 |
| α-helix | 264-266 | 3 | |
| β-strand | 267-273 | 7 | 6 |
| β-strand | 274 | 1 | 9 |
| β-strand | 279-285 | 7 | 6 |
| α-helix | 293-298 | 6 | |
| α-helix | 301-310 | 10 | |
| β-strand | 312-319 | 8 | 6 |
| β-strand | 321-322 | 2 | 10 |
| β-strand | 323-330 | 8 | 7 |
| α-helix | 332-337 | 6 | |
| β-strand | 355 | 1 | 8 |
| β-strand | 364-375 | 12 | 7 |
| β-strand | 379-390 | 12 | 7 |
| β-strand | 408-414 | 7 | 6 |
| β-strand | 419-426 | 8 | 6 |
| 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) |
>1DZH_1 ANTITHROMBIN-III (chains I) HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH FFFAKLNCRLYRKAQKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD DLYVSDAFHKAFLEVNEEGCEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI IFMGRVANPCVK
>1DZH_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 | 3 |
Water and common crystallization additives (GOL) are not listed.
The Conformational Activation of Antithrombin. A 2. 85-A Structure of a Fluorescein Derivative Reveals an Electrostatic Link between the Hinge and Heparin Binding Regions. Huntington, J.A., Mccoy, A.J., Belzar, K.J. et al. J Biol Chem (2000) 275:15377. DOI 10.1074/JBC.275.20.15377 · 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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