1UVT: Bovine thrombin--BM14.1248 complex

Bovine thrombin--BM14.1248 complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Nov 1997.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Bos taurus
Chains
2
Atoms
2,247
Mol. weight
35.89 kDa
Ligands
I48
Released
19 Nov 1997

Explore 1UVT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UVT contains 10 α-helices and 23 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 H: 9 helices, 23 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3563
β-strand39-4683
β-strand51-5443
α-helix56-583
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
β-strand12212
α-helix123-1242
α-helix126-129C7
β-strand135-14062
β-strand15415
β-strand156-16272
α-helix163-1642
α-helix165-1706
β-strand180-18342
α-helix186-186B3
β-strand18911
β-strand198-20362
β-strand206-21382
β-strand226-23052
α-helix231-2344
Chain L: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix14C-14J8

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ThrombinLprotein49Bos taurusP00735 (AlphaFold model)
ThrombinHprotein259Bos taurusP00735 (AlphaFold model)
Sequence of entity 1 (L), FASTA
>1UVT_1 THROMBIN (chains L)
TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR
Sequence of entity 2 (H), FASTA
>1UVT_2 THROMBIN (chains H)
IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL
VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL
PDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIR
ITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDRLGS

Ligands and cofactors

IDNameFormulaCopies
I48N-{3-methyl-5-[2-(pyridin-4-ylamino)-ethoxy]-phenyl}-benzenesulfonamideC20 H22 N3 O3 S1

Primary citation

Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: implications for drug design. Engh, R.A., Brandstetter, H., Sucher, G. et al. Structure (1996) 4:1353-1362. DOI 10.1016/S0969-2126(96)00142-6 · PubMed

Other PDB entries of the same protein (UniProt P00735 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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