1DX5: Thrombin-thrombomodulin complex
Crystal structure of the thrombin-thrombomodulin complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Apr 2000.
- Method
- X-ray diffraction
- Resolution
- 2.3 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 14,018
- Mol. weight
- 194.11 kDa
- Ligands
- 0GJ, NAG, CA
- Released
- 10 Apr 2000
Explore 1DX5 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1DX5 contains 64 α-helices and 140 β-strands across 12 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.
Chains A and D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14I | 7 | |
Chains B and C: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-10 | 3 | |
| α-helix | 14C-14H | 6 | |
Chain I: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 350-353 | 4 | |
| β-strand | 359-362 | 4 | 1 |
| β-strand | 368-371 | 4 | 1 |
| β-strand | 376-379 | 4 | 2 |
| β-strand | 382-388 | 7 | 2 |
| β-strand | 394-396 | 3 | 3 |
| β-strand | 398-399 | 2 | 4 |
| β-strand | 407-408 | 2 | 4 |
| β-strand | 413-416 | 4 | 3 |
| β-strand | 420-423 | 4 | 3 |
| α-helix | 426-429 | 4 | |
| β-strand | 436-439 | 4 | 5 |
| β-strand | 444-448 | 5 | 5 |
| β-strand | 455-458 | 4 | 5 |
Chain J: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 350-353 | 4 | |
| β-strand | 359-362 | 4 | 6 |
| β-strand | 368-371 | 4 | 6 |
| β-strand | 376-379 | 4 | 7 |
| β-strand | 382-388 | 7 | 7 |
| β-strand | 394-396 | 3 | 8 |
| β-strand | 398-399 | 2 | 9 |
| β-strand | 407-408 | 2 | 9 |
| β-strand | 413-416 | 4 | 8 |
| β-strand | 420-423 | 4 | 8 |
| α-helix | 426-429 | 4 | |
| β-strand | 436-439 | 4 | 10 |
| β-strand | 444-447 | 4 | 10 |
| β-strand | 456-458 | 3 | 10 |
Chain K: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 350-353 | 4 | |
| β-strand | 359-362 | 4 | 11 |
| β-strand | 368-371 | 4 | 11 |
| β-strand | 376-379 | 4 | 12 |
| β-strand | 382-388 | 7 | 12 |
| β-strand | 394-396 | 3 | 13 |
| β-strand | 398-400 | 3 | 14 |
| β-strand | 406-408 | 3 | 14 |
| β-strand | 413-416 | 4 | 13 |
| β-strand | 420-423 | 4 | 13 |
| α-helix | 426-429 | 4 | |
| β-strand | 436-439 | 4 | 15 |
| β-strand | 444-447 | 4 | 15 |
| β-strand | 456-458 | 3 | 15 |
Chain L: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 350-353 | 4 | |
| β-strand | 359-362 | 4 | 16 |
| β-strand | 368-371 | 4 | 16 |
| β-strand | 376-379 | 4 | 17 |
| β-strand | 382-388 | 7 | 17 |
| β-strand | 394-396 | 3 | 18 |
| β-strand | 398-400 | 3 | 19 |
| β-strand | 406-408 | 3 | 19 |
| β-strand | 413-416 | 4 | 18 |
| β-strand | 420-423 | 4 | 18 |
| α-helix | 426-429 | 4 | |
| β-strand | 436-439 | 4 | 20 |
| β-strand | 444-447 | 4 | 20 |
| β-strand | 457-458 | 2 | 20 |
Chain M: 12 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17 | 1 | 21 |
| β-strand | 20-21 | 2 | 22 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 23 |
| β-strand | 39-46 | 8 | 23 |
| β-strand | 51-54 | 4 | 23 |
| α-helix | 56-58 | 3 | |
| β-strand | 60-60A | 2 | 24 |
| α-helix | 60B-60D | 3 | |
| β-strand | 60F-60G | 2 | 24 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 23 |
| β-strand | 72 | 1 | 25 |
| β-strand | 81-83 | 3 | 23 |
| β-strand | 85-90 | 6 | 23 |
| β-strand | 95 | 1 | 26 |
| β-strand | 100 | 1 | 26 |
| β-strand | 104-108 | 5 | 23 |
| α-helix | 111-114 | 4 | |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 22 |
| α-helix | 126-129C | 7 | |
| β-strand | 135-140 | 6 | 22 |
| β-strand | 154 | 1 | 25 |
| β-strand | 156-162 | 7 | 22 |
| α-helix | 165-170 | 6 | |
| α-helix | 175-177 | 3 | |
| β-strand | 180-183 | 4 | 22 |
| α-helix | 186-186B | 3 | |
| β-strand | 189 | 1 | 21 |
| β-strand | 198-202 | 5 | 22 |
| β-strand | 207-215 | 9 | 22 |
| β-strand | 226-230 | 5 | 22 |
| α-helix | 232-234 | 3 | |
| α-helix | 235-244 | 10 | |
Chain N: 13 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17 | 1 | 27 |
| β-strand | 20-21 | 2 | 28 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 29 |
| β-strand | 39-46 | 8 | 29 |
| β-strand | 51-54 | 4 | 29 |
| α-helix | 56-58 | 3 | |
| β-strand | 60-60A | 2 | 30 |
| α-helix | 60B-60D | 3 | |
| β-strand | 60F-60G | 2 | 30 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-68 | 5 | 29 |
| β-strand | 72 | 1 | 31 |
| β-strand | 81-83 | 3 | 29 |
| β-strand | 85-90 | 6 | 29 |
| β-strand | 95 | 1 | 32 |
| β-strand | 100 | 1 | 32 |
| β-strand | 104-108 | 5 | 29 |
| α-helix | 111-114 | 4 | |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 28 |
| α-helix | 123-124 | 2 | |
| α-helix | 126-129C | 7 | |
| β-strand | 135-140 | 6 | 28 |
| β-strand | 154 | 1 | 31 |
| β-strand | 156-162 | 7 | 28 |
| α-helix | 165-170 | 6 | |
| α-helix | 175-176 | 2 | |
| β-strand | 180-183 | 4 | 28 |
| α-helix | 186-186B | 3 | |
| β-strand | 189 | 1 | 27 |
| β-strand | 198-202 | 5 | 28 |
| β-strand | 207-215 | 9 | 28 |
| β-strand | 226-230 | 5 | 28 |
| α-helix | 232-234 | 3 | |
| α-helix | 235-244 | 10 | |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Thrombin light chain | A, B, C, D | protein | 36 | Homo sapiens | P00734 (AlphaFold model) |
| Thrombomodulin | I, J, K, L | protein | 118 | Homo sapiens | P07204 (AlphaFold model) |
| Thrombin heavy chain | M, N, O, P | protein | 259 | Homo sapiens | P00734 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>1DX5_1 Thrombin light chain (chains A, B, C, D)
TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
Sequence of entity 2 (I, J, K, L), FASTA
>1DX5_2 Thrombomodulin (chains I, J, K, L)
VEPVDPCFRANCEYQCQPLDQTSYLCVCAEGFAPIPHEPHRCQMFCNQTACPADCDPNTQ
ASCECPEGYILDDGFICTDIDECENGGFCSGVCHNLPGTFECICGPDSALAGQIGTDC
Sequence of entity 3 (M, N, O, P), FASTA
>1DX5_3 Thrombin heavy chain (chains M, N, O, P)
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFIENDLL
VRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL
PDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIR
ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDQFGE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 0GJ | L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydr… | C14 H28 Cl N6 O5 | 16 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 4 |
| CA | Calcium ion | Ca | 4 |
Water and common crystallization additives (NA, FMT) are not listed.
Primary citation
Structural Basis for the Anticoagulant Activity of the Thrombin-Thrombomodulin Complex. Fuentes-Prior, P., Iwanaga, Y., Huber, R. et al. Nature (2000) 404:518. DOI 10.1038/35006683 · PubMed
Other PDB entries of the same protein (UniProt P00734 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5AFY 1.12 Å, Thrombin in complex with 3-chloro-benzamide
- 4UD9 1.12 Å, Thrombin in complex with 5-chlorothiophene-2-carboxamide
- 4UE7 1.13 Å, Thrombin in complex with 1-amidinopiperidine
- 4UDW 1.16 Å, Thrombin in complex with 1-(2R)-2-amino-3-phenyl-propanoyl-N-(2,…
- 4UEH 1.16 Å, Thrombin in complex with benzamidine
- 5AF9 1.18 Å, Thrombin in complex with 4-Methoxy-N-(2-pyridinyl)benzamide
- 3RM2 1.23 Å, Human Thrombin in complex with MI003
- 5AHG 1.24 Å, Thrombin in complex with ((4-chlorophenyl)sulfamoyl))diemethylamine
- 2BVR 1.25 Å, Human thrombin complexed with fragment-based small molecules occupying the S1 pocket
- 3VXE 1.25 Å, Human alpha-thrombin-Bivalirudin complex at PD5.0
- 2UUF 1.26 Å, Thrombin-hirugen binary complex at 1.26A resolution
- 3SI4 1.27 Å, Human Thrombin In Complex With UBTHR104
Browse structure collections
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