1MKW: 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 2.3 Å resolution. Released 7 Jul 1997.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Bos taurus
Chains
3
Atoms
4,838
Mol. weight
71 kDa
Released
7 Jul 1997

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

Secondary structure: helices and β-sheets

1MKW contains 24 α-helices and 45 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: 10 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3673
β-strand38-4693
β-strand51-5443
α-helix56-583
β-strand60-60A24
α-helix60B-60D3
β-strand60F-60G24
β-strand64-6963
α-helix77A-793
β-strand80-8343
β-strand85-9063
β-strand9515
β-strand10015
β-strand104-10853
α-helix120-1212
β-strand12212
α-helix123-1242
α-helix126-129C7
β-strand135-14062
β-strand156-16272
α-helix165-1706
β-strand180-18342
α-helix186-186B3
β-strand18911
β-strand198-20252
β-strand207-21592
β-strand226-23052
α-helix235-2428
Chain K: 12 helices, 24 β-strands
ElementResiduesLengthSheet
α-helix8-103
α-helix14C-14J8
β-strand19-2136
α-helix22-232
β-strand30-3567
β-strand39-4687
β-strand51-5447
α-helix56-583
β-strand60-60A28
α-helix60B-60D3
β-strand60F-60G28
β-strand64-6857
β-strand7219
β-strand81-90107
β-strand95110
β-strand100110
β-strand104-10857
β-strand115111
β-strand118111
α-helix120-1212
β-strand12216
α-helix123-1242
α-helix126-129C7
β-strand135-14066
β-strand15419
β-strand156-16166
β-strand162112
α-helix165-1706
β-strand180-183412
α-helix184A-1852
β-strand198-20256
β-strand207-21266
β-strand213112
β-strand226-229412
α-helix232-2343
α-helix235-2428
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
>1MKW_1 ALPHA-THROMBIN (chains L)
TSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR
Sequence of entity 2 (H), FASTA
>1MKW_2 ALPHA-THROMBIN (chains H)
IVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLL
VRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCL
PDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIR
ITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFY
THVFRLKKWIQKVIDRLGS
Sequence of entity 3 (K), FASTA
>1MKW_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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