Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 Jul 2003.
Explore 1OOK in 3D Show helices and sheets RCSB PDB PDBe
1OOK contains 19 α-helices and 42 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14H | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 3 |
| β-strand | 39-46 | 8 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 60-60A | 2 | 4 |
| α-helix | 60B-60D | 3 | |
| β-strand | 60F-60G | 2 | 4 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 5 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 95 | 1 | 6 |
| β-strand | 100 | 1 | 6 |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| α-helix | 126-129C | 7 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 151 | 1 | 7 |
| β-strand | 154 | 1 | 5 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-169 | 5 | |
| α-helix | 175-176 | 2 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-202 | 5 | 2 |
| β-strand | 207-215 | 9 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 232-234 | 3 | |
| α-helix | 235-242 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 8 |
| β-strand | 12-16 | 5 | 8 |
| β-strand | 33-37 | 5 | 8 |
| β-strand | 45-47 | 3 | 9 |
| α-helix | 48-51 | 4 | |
| β-strand | 59-61 | 3 | 8 |
| β-strand | 69-71 | 3 | 9 |
| β-strand | 81-83 | 3 | 8 |
| β-strand | 104-106 | 3 | 8 |
| β-strand | 128-130 | 3 | 8 |
| α-helix | 139-140 | 2 | |
| β-strand | 152-154 | 3 | 8 |
| β-strand | 176-178 | 3 | 8 |
| β-strand | 199-201 | 3 | 8 |
| β-strand | 207 | 1 | 10 |
| α-helix | 214-222 | 9 | |
| α-helix | 224-226 | 3 | |
| β-strand | 227 | 1 | 8 |
| α-helix | 243-245 | 3 | |
| β-strand | 247 | 1 | 11 |
| β-strand | 248 | 1 | 10 |
| β-strand | 255 | 1 | 11 |
| α-helix | 256-258 | 3 | |
| β-strand | 282 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human Alpha Thrombin | A | protein | 36 | Homo sapiens | P00734 (AlphaFold model) |
| Human Alpha Thrombin | B | protein | 259 | Homo sapiens | P00734 (AlphaFold model) |
| PHE-PRO-ARG-Chloromethylketone | P | protein | 3 | ||
| Platelet glycoprotein Ib alpha chain precursor | G | protein | 290 | Homo sapiens | P07359 (AlphaFold model) |
>1OOK_1 Human Alpha Thrombin (chains A) TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
>1OOK_2 Human Alpha Thrombin (chains B) IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLL VRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL PDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIR ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQFGE
>1OOK_3 PHE-PRO-ARG-Chloromethylketone (chains P) FPR
>1OOK_4 Platelet glycoprotein Ib alpha chain precursor (chains G) HPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQL NLDRAELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGAL RGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQ ENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMT SNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Water and common crystallization additives (CL) are not listed.
Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha. Celikel, R., McClintock, R.A., Roberts, J.R. et al. Science (2003) 301:218-221. DOI 10.1126/science.1084183 · PubMed
Other PDB entries of the same protein (UniProt P00734 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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