Crystal structure of bovine thrombin complex with protease inhibitor ecotin. Determined by X-ray diffraction at 2.5 Å resolution. Released 5 Sept 2001.
Explore 1ID5 in 3D Show helices and sheets RCSB PDB PDBe
1ID5 contains 19 α-helices and 29 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 | 30-35 | 6 | 3 |
| β-strand | 39-46 | 8 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 111-114 | 4 | |
| 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 | 4 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-202 | 5 | 2 |
| β-strand | 207-216 | 10 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-243 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| α-helix | 13-16 | 4 | |
| β-strand | 20-25 | 6 | 2 |
| α-helix | 27-29 | 3 | |
| α-helix | 33-35 | 3 | |
| β-strand | 36-47 | 12 | 5 |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 55 | 1 | 6 |
| β-strand | 56-64 | 9 | 2 |
| β-strand | 69-83 | 15 | 2 |
| β-strand | 94-98 | 5 | 5 |
| β-strand | 99 | 1 | 6 |
| α-helix | 102-105 | 4 | |
| β-strand | 106-108 | 3 | 5 |
| α-helix | 109 | 1 | |
| β-strand | 115-120 | 6 | 2 |
| β-strand | 124-131 | 8 | 5 |
| α-helix | 132-133 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14J | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thrombin | L | protein | 49 | Bos taurus | P00735 (AlphaFold model) |
| Thrombin | H | protein | 256 | Bos taurus | P00735 (AlphaFold model) |
| Ecotin | I | protein | 142 | Escherichia coli | P23827 (AlphaFold model) |
>1ID5_1 THROMBIN (chains L) TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR
>1ID5_2 THROMBIN (chains H) IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL PDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIR ITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDR
>1ID5_3 ECOTIN (chains I) AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE NKTLEGWGYDYYVFDKVSSPVSTRMACPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP DNVDVKYRVWKAEEKIDNAVVR
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (TRS) are not listed.
Crystal structure of thrombin-ecotin reveals conformational changes and extended interactions. Wang, S.X., Esmon, C.T., Fletterick, R.J. Biochemistry (2001) 40:10038-10046. DOI 10.1021/bi010712h · 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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