2A32: Trypsin

Trypsin in complex with benzene boronic acid. Determined by X-ray diffraction at 1.5 Å resolution. Released 4 Jul 2006.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Sus scrofa
Chains
1
Atoms
2,121
Mol. weight
24.44 kDa
Ligands
CA, PG3, PBC, BO4
Released
4 Jul 2006

Explore 2A32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A32 contains 8 α-helices and 18 β-strands across 1 chain. 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 A: 8 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3453
β-strand40-4893
β-strand51-5443
α-helix56-583
β-strand64-6743
β-strand7214
β-strand81-90103
β-strand104-10853
β-strand12212
α-helix123-1242
α-helix128-1303
β-strand135-14062
β-strand15414
β-strand156-16272
α-helix163-1642
α-helix165-1717
β-strand180-18342
β-strand18911
β-strand198-20142
β-strand204-21582
β-strand226-23052
α-helix231-2333
α-helix235-2439

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TrypsinAprotein223Sus scrofaP00761 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2A32_1 Trypsin (chains A)
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEG
NEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISG
WGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGP
VVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1
PG3Guanidine-3-propanolC4 H12 N3 O1
PBCPhenyl boronic acidC6 H7 B O22
BO4Borate ionB H4 O41
CXS3-cyclohexyl-1-propylsulfonic acidC9 H19 N O3 S2

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

Primary citation

NMR and crystallographic characterization of adventitious borate binding by trypsin. Transue, T.R., Gabel, S.A., London, R.E. Bioconjug Chem (2006) 17:300-308. DOI 10.1021/bc0502210 · PubMed

Other PDB entries of the same protein (UniProt P00761 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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