Crystallographic structures of Thrombin complexed with Thrombin receptor peptides: Existence of expected and novel binding modes. Determined by X-ray diffraction at 2.4 Å resolution. Released 31 May 1994.
Explore 1NRR in 3D Show helices and sheets RCSB PDB PDBe
1NRR contains 15 α-helices and 22 β-strands across 3 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 | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-36 | 7 | 3 |
| β-strand | 38-46 | 9 | 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 | 111-114 | 4 | |
| 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 | 154 | 1 | 5 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 165-170 | 6 | |
| β-strand | 180-183 | 4 | 2 |
| α-helix | 186-186B | 3 | |
| 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 | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14H | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 52-54 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thrombin light chain | L | protein | 36 | Homo sapiens | P00734 (AlphaFold model) |
| Thrombin heavy chain | H | protein | 259 | Homo sapiens | P00734 (AlphaFold model) |
| Proteinase-activated receptor 1 | R | protein | 18 | Homo sapiens | P25116 (AlphaFold model) |
>1NRR_1 Thrombin light chain (chains L) TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
>1NRR_2 Thrombin heavy chain (chains H) IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLL VRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL PDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIR ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQFGE
>1NRR_3 Proteinase-activated receptor 1 (chains R) FLLRNPNDKYEPFWEDEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| 0G6 | D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexa… | C21 H34 Cl N6 O3 | 1 |
Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. Mathews, I.I., Padmanabhan, K.P., Ganesh, V. et al. Biochemistry (1994) 33:3266-3279. DOI 10.1021/bi00177a018 · 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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