2F9O: Recombinant Human Alpha I Tryptase Mutant D216G

Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Jan 2006.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
4
Atoms
8,745
Mol. weight
111.78 kDa
Released
31 Jan 2006

Explore 2F9O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F9O contains 40 α-helices and 104 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.

Chains A and C: 10 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3673
β-strand38-48113
β-strand51-5443
α-helix56-583
β-strand60B14
α-helix61-633
β-strand64-6743
β-strand7215
β-strand8313
β-strand85-9063
α-helix97-993
β-strand104-10853
α-helix111-1144
β-strand12212
α-helix123-1253
β-strand136-14052
β-strand14516
β-strand14916
α-helix150-1523
β-strand15415
β-strand156-15942
β-strand162-16322
α-helix165-1739
β-strand173C17
β-strand180-18342
β-strand18911
β-strand198-20362
β-strand206-215102
β-strand221A18
β-strand22418
β-strand226-23052
α-helix231-2344
α-helix235-2384
Chain B: 10 helices, 26 β-strands
ElementResiduesLengthSheet
β-strand1719
β-strand20-21210
α-helix22-232
β-strand30-37811
β-strand37B-481211
β-strand51-54411
α-helix56-583
β-strand60B112
α-helix61-633
β-strand64-67411
β-strand72113
β-strand83111
β-strand85-90611
α-helix97-993
β-strand104-108511
α-helix111-1144
β-strand122110
α-helix123-1253
β-strand136-140510
β-strand145114
β-strand149114
α-helix150-1523
β-strand154113
β-strand156-159410
β-strand162-163210
α-helix165-1739
β-strand173C115
β-strand180-183410
β-strand18919
β-strand198-203610
β-strand206-2151010
β-strand221A116
β-strand224116
β-strand226-230510
α-helix231-2344
α-helix235-2417
Chain D: 10 helices, 26 β-strands
ElementResiduesLengthSheet
β-strand17123
β-strand20-21224
α-helix22-232
β-strand30-37825
β-strand37B-481225
β-strand51-54425
α-helix56-583
β-strand60B17
α-helix61-633
β-strand64-67425
β-strand72126
β-strand83125
β-strand85-90625
α-helix97-993
β-strand104-108525
α-helix111-1144
β-strand122124
α-helix123-1253
β-strand136-140524
β-strand145127
β-strand149127
α-helix150-1523
β-strand154126
β-strand156-159424
β-strand162-163224
α-helix165-1739
β-strand173C14
β-strand180-183424
β-strand189123
β-strand198-203624
β-strand206-2151024
β-strand221A128
β-strand224128
β-strand226-230524
α-helix231-2344
α-helix235-2395

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tryptase alpha-1A, B, C, Dprotein245Homo sapiensQ15661 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2F9O_1 Tryptase alpha-1 (chains A, B, C, D)
IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLATLRVQL
REQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEPVNISSRVHTVMLPPASETFP
PGMPCWVTGWGDVDNDEPLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIIRDDML
CAGNSQRDSCKGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPKKP

Primary citation

X-ray Structures of Free and Leupeptin-complexed Human alpha I-Tryptase Mutants: Indication for an alpha to beta-Tryptase Transition. Rohr, K.B., Selwood, T., Marquardt, U. et al. J Mol Biol (2005) 357:195-209. DOI 10.1016/j.jmb.2005.12.037 · PubMed

Other PDB entries of the same protein (UniProt Q15661 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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