3BEF: Thrombin

Crystal structure of thrombin bound to the extracellular fragment of PAR1. Determined by X-ray diffraction at 2.2 Å resolution. Released 1 Jan 2008.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
6
Atoms
5,186
Mol. weight
73.19 kDa
Ligands
NAG
Released
1 Jan 2008

Explore 3BEF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BEF contains 30 α-helices and 46 β-strands across 5 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.

Chain A: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix1J-1G4
α-helix1C-1A3
α-helix8-103
α-helix14C-14H6
Chain B: 11 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3563
β-strand39-4683
β-strand51-5443
α-helix56-594
β-strand60-60A24
α-helix60B-60D3
β-strand60F-60G24
β-strand64-6853
β-strand7215
β-strand81-8333
β-strand85-9063
β-strand9516
β-strand10016
β-strand104-10853
α-helix111-1144
α-helix120-1212
β-strand12212
α-helix123-1253
α-helix126-129C7
β-strand135-14062
β-strand15415
β-strand156-16272
α-helix165-1706
α-helix175-1762
β-strand180-18342
β-strand18911
β-strand198-20252
β-strand207-21592
β-strand226-23052
α-helix232-2343
α-helix235-2428
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix52-543
Chain D: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1J-1G4
α-helix1C-1A3
α-helix8-103
α-helix14C-14K9
Chain E: 10 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand1717
β-strand20-2128
α-helix22-232
β-strand30-3569
β-strand39-4689
β-strand51-5449
α-helix56-583
β-strand60110
β-strand60G110
α-helix61-633
β-strand64-6859
β-strand72111
β-strand81-8339
β-strand85-9069
β-strand95112
β-strand100112
β-strand104-10859
α-helix111-1144
α-helix120-1212
β-strand12218
α-helix123-1242
α-helix126-129C7
β-strand135-14068
β-strand154111
β-strand156-16278
α-helix165-1717
β-strand180-18348
β-strand18917
β-strand198-20258
β-strand207-21378
β-strand226-23058
α-helix231-2344
α-helix235-2428

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ProthrombinA, Dprotein46Homo sapiensP00734 (AlphaFold model)
ProthrombinB, Eprotein259Homo sapiensP00734 (AlphaFold model)
Proteinase-activated receptor 1C, Fprotein9Homo sapiensP25116 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>3BEF_1 Prothrombin (chains A, D)
SEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
Sequence of entity 2 (B, E), FASTA
>3BEF_2 Prothrombin (chains B, E)
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLL
VRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRNIALMKLKKPVAFSDYIHPVCL
PDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIR
ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDQFGE
Sequence of entity 3 (C, F), FASTA
>3BEF_3 Proteinase-activated receptor 1 (chains C, F)
NDKYEPFWE

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

Primary citation

Structural identification of the pathway of long-range communication in an allosteric enzyme. Gandhi, P.S., Chen, Z., Mathews, F.S. et al. Proc Natl Acad Sci U S A (2008) 105:1832-1837. DOI 10.1073/pnas.0710894105 · 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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