5TO3: Prothrombin

Crystal structure of thrombin mutant W215A/E217A fused to EGF456 of thrombomodulin via a 31-residue linker and bound to PPACK. Determined by X-ray diffraction at 2.34 Å resolution. Released 29 Mar 2017.

Method
X-ray diffraction
Resolution
2.34 Å
Organism
Homo sapiens
Chains
2
Atoms
3,477
Mol. weight
52.18 kDa
Ligands
NAG, 0G6
Released
29 Mar 2017

Explore 5TO3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TO3 contains 19 α-helices and 35 β-strands across 2 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-helix10-134
α-helix17-193
α-helix27-293
α-helix36-438
Chain B: 15 helices, 35 β-strands
ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3563
β-strand40-4783
β-strand52-5543
α-helix57-604
β-strand61-6224
α-helix63-653
β-strand67-6824
α-helix71-733
β-strand74-7853
β-strand8215
β-strand92-9433
β-strand96-10163
β-strand10616
β-strand11216
β-strand116-12053
α-helix123-1264
α-helix132-1332
β-strand13412
α-helix135-1362
α-helix138-1447
β-strand150-15562
β-strand17415
β-strand176-18382
α-helix185-1906
β-strand200-20342
α-helix207-2093
β-strand21411
β-strand223-22752
β-strand234-24292
β-strand253-25752
α-helix259-2613
α-helix262-27211
α-helix350-3523
β-strand359-36247
β-strand368-37147
β-strand376-37948
β-strand382-38878
β-strand394-39639
β-strand398-400310
α-helix401-4033
β-strand405-408410
β-strand413-41649
β-strand420-42349
α-helix426-4294
β-strand436-440511
β-strand443-447511
β-strand456-458311

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ProthrombinAprotein46Homo sapiensP00734 (AlphaFold model)
Prothrombin,ThrombomodulinBprotein409Homo sapiensP00734 (AlphaFold model), P07204 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5TO3_1 Prothrombin (chains A)
SEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
Sequence of entity 2 (B), FASTA
>5TO3_2 Prothrombin,Thrombomodulin (chains B)
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLL
VRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCL
PDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIR
ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSAGAGCDRDGKYGFY
THVFRLKKWIQKVIDQFGGGSSSAGGGSSSGGGGSSSAGGGSSSGGGGVEPVDPCFRANC
EYQCQPLNQTSYLCVCAEGFAPIPHEPHRCQMFCNQTACPADCDPNTQASCECPEGYILD
DGFICTDIDECENGGFCSGVCHNLPGTFECICGPDSALARHIGTDCDSG

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62
0G6D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexa…C21 H34 Cl N6 O31

Water and common crystallization additives (NA, K) are not listed.

Primary citation

Rational Design of Protein C Activators. Barranco-Medina, S., Murphy, M., Pelc, L. et al. Sci Rep (2017) 7:44596-44596. DOI 10.1038/srep44596 · PubMed

Other PDB entries of the same protein (UniProt P00734 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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