1MKX: Alpha-thrombin

The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the yppw segment and active site residues upon ligand binding. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Jul 1997.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Bos taurus
Chains
3
Atoms
5,012
Mol. weight
71 kDa
Released
7 Jul 1997

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

Secondary structure: helices and β-sheets

1MKX contains 25 α-helices and 46 β-strands across 3 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
α-helix120-1212
β-strand12212
α-helix123-1242
α-helix126-129C7
β-strand135-14062
β-strand15415
β-strand156-16272
α-helix165-1706
β-strand180-18342
α-helix186-186B3
β-strand18911
β-strand198-20252
β-strand207-21592
β-strand226-23052
α-helix231-24010
Chain K: 14 helices, 23 β-strands
ElementResiduesLengthSheet
α-helix5-95
α-helix14C-14J8
β-strand19-2137
α-helix22-232
β-strand30-3568
β-strand39-4688
β-strand51-5448
α-helix56-583
β-strand60-60A29
α-helix60B-60D3
β-strand60F-60G29
α-helix61-633
β-strand64-6858
β-strand72110
β-strand81-8338
β-strand85-9068
β-strand95111
β-strand100111
β-strand104-10858
α-helix111-1144
β-strand115112
β-strand118112
α-helix120-1212
β-strand12217
α-helix123-1242
α-helix126-129C7
β-strand135-14067
β-strand154110
β-strand156-16277
α-helix165-1706
α-helix175-1762
β-strand180-18347
α-helix1941
β-strand198-20257
β-strand207-21377
β-strand226-23057
α-helix231-24212
Chain L: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix8-103
α-helix14C-14J8

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-thrombinLprotein49Bos taurusP00735 (AlphaFold model)
Alpha-thrombinHprotein259Bos taurusP00735 (AlphaFold model)
Prethrombin-2Kprotein308Bos taurusP00735 (AlphaFold model)
Sequence of entity 1 (L), FASTA
>1MKX_1 ALPHA-THROMBIN (chains L)
TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR
Sequence of entity 2 (H), FASTA
>1MKX_2 ALPHA-THROMBIN (chains H)
IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL
VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL
PDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIR
ITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDRLGS
Sequence of entity 3 (K), FASTA
>1MKX_3 PRETHROMBIN-2 (chains K)
TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGL
SPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRY
ERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLH
AGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYK
PGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQ
KVIDRLGS

Primary citation

The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand binding. Malkowski, M.G., Martin, P.D., Guzik, J.C. et al. Protein Sci (1997) 6:1438-1448. 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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