9T00: Prothrombin

Crystal structure of prethrombin-2 with a peptide corresponding to the C-terminus of the heavy chain of factor Va. Determined by X-ray diffraction at 2.8 Å resolution. Released 12 Aug 2026.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
4
Atoms
5,125
Mol. weight
77.9 kDa
Released
12 Aug 2026

Explore 9T00 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9T00 contains 35 α-helices and 42 β-strands across 4 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: 17 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix283-2864
α-helix290-2923
α-helix300-3023
α-helix309-3113
α-helix313-3153
β-strand325-32621
α-helix327-3282
β-strand335-34062
β-strand346-35272
β-strand357-36042
α-helix362-3654
β-strand366-36723
α-helix368-3703
β-strand372-37323
α-helix376-3783
β-strand379-38352
β-strand38714
β-strand397-39932
β-strand401-40662
β-strand41115
β-strand41715
β-strand421-42552
α-helix437-4382
β-strand43911
α-helix443-4497
β-strand455-46061
α-helix463-4686
β-strand47914
β-strand481-48771
α-helix488-4892
α-helix490-4956
β-strand505-50841
α-helix5241
β-strand528-53251
β-strand539-54571
β-strand558-56251
α-helix564-5663
α-helix567-5759
Chains B and D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix693-70513
Chain C: 16 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix283-2864
α-helix290-2923
α-helix300-3023
α-helix308-3114
β-strand325-32626
α-helix327-3282
β-strand335-34067
β-strand345-35287
β-strand357-36047
α-helix362-3654
β-strand366-36728
α-helix368-3703
β-strand372-37328
α-helix376-3783
β-strand379-38357
β-strand38719
β-strand397-39937
β-strand401-40667
β-strand411110
β-strand417110
β-strand421-42557
α-helix437-4382
β-strand43916
α-helix443-4497
β-strand455-46066
α-helix463-4686
β-strand47919
β-strand481-48776
α-helix488-4892
α-helix490-4956
β-strand505-50846
α-helix5241
β-strand528-53256
β-strand539-54576
β-strand558-56256
α-helix564-5663
α-helix567-5759

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ProthrombinA, Cprotein314Homo sapiensP00734 (AlphaFold model)
Coagulation factor V heavy chainB, Dprotein24Homo sapiensP12259 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>9T00_1 Prothrombin (chains A, C)
MAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGS
DAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGK
HSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRET
AASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNM
FCAGYKPDEGKRGDACEGDAGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFR
LKKWIQKVIDQFGE
Sequence of entity 2 (B, D), FASTA
>9T00_2 Coagulation factor V heavy chain (chains B, D)
EPEDEESDADYDYQNRLAAALGIR

Primary citation

Prothrombinase processivity is conferred by substrate allostery. Ustok, F.I., Faille, A., Warren, A.J. et al. EMBO J (2026) 45:3954-3977. DOI 10.1038/s44318-026-00782-4 · 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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