3EDX: W215A/E217A mutant of murine thrombin

Crystal structure of the W215A/E217A mutant of murine thrombin. Determined by X-ray diffraction at 2.4 Å resolution. Released 7 Jul 2009.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Mus musculus
Chains
6
Atoms
7,612
Mol. weight
106.04 kDa
Ligands
NAG
Released
7 Jul 2009

Explore 3EDX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EDX contains 48 α-helices and 64 β-strands across 6 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.

Chains A, C and E: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix1J-1G4
α-helix8-103
α-helix14C-14G5
Chain B: 13 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3563
β-strand39-4683
β-strand51-5443
α-helix56-594
β-strand60-60A24
α-helix60B-60D3
β-strand60F-60G24
β-strand64-6853
β-strand7215
β-strand81-90103
β-strand104-10853
α-helix111-1144
β-strand11516
β-strand11816
α-helix120-1212
β-strand12212
α-helix123-1242
α-helix126-129C7
β-strand135-14062
α-helix149C-149E3
β-strand15415
β-strand156-16382
α-helix1641
α-helix165-1695
β-strand180-18342
β-strand18911
α-helix192-1943
β-strand198-20252
β-strand207-21592
β-strand221A17
β-strand226-23052
α-helix231-2344
α-helix235-24410
Chain D: 13 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand1718
β-strand20-2129
α-helix22-232
β-strand30-35610
β-strand39-46810
β-strand51-54410
α-helix56-583
β-strand60-60A211
α-helix60B-60D3
β-strand60F-60G211
β-strand64-68510
β-strand72112
β-strand81-901010
β-strand104-108510
α-helix111-1144
α-helix120-1212
β-strand12219
α-helix123-1242
α-helix126-129C7
β-strand135-14069
α-helix149C-1504
β-strand154112
β-strand156-16279
α-helix163-1642
α-helix165-1695
β-strand180-18349
β-strand18918
α-helix192-1943
β-strand198-20259
β-strand207-21599
β-strand226-23059
α-helix232-2343
α-helix235-24410
Chain F: 13 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand17113
β-strand20-21214
α-helix22-232
β-strand30-35615
β-strand39-46815
β-strand51-54415
α-helix56-594
β-strand60-60A216
α-helix60B-60D3
β-strand60F-60G216
β-strand64-68515
β-strand72117
β-strand81-901015
β-strand104-108515
α-helix111-1144
α-helix120-1212
β-strand122114
α-helix123-1242
α-helix126-129C7
β-strand135-140614
α-helix149C-1504
β-strand154117
β-strand156-162714
α-helix163-1642
α-helix165-1717
β-strand180-183414
β-strand189113
α-helix192-1943
β-strand198-202514
β-strand207-215914
β-strand221A17
β-strand226-230514
α-helix231-2344
α-helix235-24410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Thrombin light chainA, C, Eprotein44Mus musculusP19221 (AlphaFold model)
Thrombin heavy chainB, D, Fprotein258Mus musculusP19221 (AlphaFold model)
Sequence of entity 1 (A, C, E), FASTA
>3EDX_1 Thrombin light chain (chains A, C, E)
FHTFFNEKTFGLGEADCGLRPLFEKKSLKDTTEKELLDSYIDGR
Sequence of entity 2 (B, D, F), FASTA
>3EDX_2 Thrombin heavy chain (chains B, D, F)
IVEGWDAEKGIAPWQVMLFRKSPQELLCGASLISDRWVLTAAHCILYPPWDKNFTENDLL
VRIGKHSRTRYERNVEKISMLEKIYVHPRYNWRENLDRDIALLKLKKPVPFSDYIHPVCL
PDKQTVTSLLRAGYKGRVTGWGNLRETWTTNINEIQPSVLQVVNLPIVERPVCKASTRIR
ITDNMFCAGFKVNDTKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSAGAGCDRKGKYGFY
THVFRLKRWIQKVIDQFG

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63

Water and common crystallization additives (SO4) are not listed.

Primary citation

Molecular Basis for the Kinetic Differences of the W215A/E217A Mutant of Human and Murine Thrombin. Gandhi, P.S., Page, M.J., Chen, Z. et al. To be published.

Other PDB entries of the same protein (UniProt P19221 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3EDX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.