The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the yppw segment and active site residues upon ligand binding. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Jul 1997.
Explore 1MKW in 3D Show helices and sheets RCSB PDB PDBe
1MKW contains 24 α-helices and 45 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 |
| β-strand | 64-69 | 6 | 3 |
| α-helix | 77A-79 | 3 | |
| β-strand | 80-83 | 4 | 3 |
| β-strand | 85-90 | 6 | 3 |
| β-strand | 95 | 1 | 5 |
| β-strand | 100 | 1 | 5 |
| 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 | 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 | 235-242 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14J | 8 | |
| β-strand | 19-21 | 3 | 6 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 7 |
| β-strand | 39-46 | 8 | 7 |
| β-strand | 51-54 | 4 | 7 |
| α-helix | 56-58 | 3 | |
| β-strand | 60-60A | 2 | 8 |
| α-helix | 60B-60D | 3 | |
| β-strand | 60F-60G | 2 | 8 |
| β-strand | 64-68 | 5 | 7 |
| β-strand | 72 | 1 | 9 |
| β-strand | 81-90 | 10 | 7 |
| β-strand | 95 | 1 | 10 |
| β-strand | 100 | 1 | 10 |
| β-strand | 104-108 | 5 | 7 |
| β-strand | 115 | 1 | 11 |
| β-strand | 118 | 1 | 11 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 6 |
| α-helix | 123-124 | 2 | |
| α-helix | 126-129C | 7 | |
| β-strand | 135-140 | 6 | 6 |
| β-strand | 154 | 1 | 9 |
| β-strand | 156-161 | 6 | 6 |
| β-strand | 162 | 1 | 12 |
| α-helix | 165-170 | 6 | |
| β-strand | 180-183 | 4 | 12 |
| α-helix | 184A-185 | 2 | |
| β-strand | 198-202 | 5 | 6 |
| β-strand | 207-212 | 6 | 6 |
| β-strand | 213 | 1 | 12 |
| β-strand | 226-229 | 4 | 12 |
| α-helix | 232-234 | 3 | |
| α-helix | 235-242 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14J | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-thrombin | L | protein | 49 | Bos taurus | P00735 (AlphaFold model) |
| Alpha-thrombin | H | protein | 259 | Bos taurus | P00735 (AlphaFold model) |
| Prethrombin-2 | K | protein | 308 | Bos taurus | P00735 (AlphaFold model) |
>1MKW_1 ALPHA-THROMBIN (chains L) TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR
>1MKW_2 ALPHA-THROMBIN (chains H) IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL PDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIR ITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDRLGS
>1MKW_3 PRETHROMBIN-2 (chains K) TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGL SPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRY ERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLH AGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYK PGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQ KVIDRLGS
The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand binding. Malkowski, M.G., Martin, P.D., Guzik, J.C. et al. Protein Sci (1997) 6:1438-1448. PubMed
Other PDB entries of the same protein (UniProt P00735 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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