9PDA: Porcine Trypsin Crystals Grown From PEG and

Structure of Porcine Trypsin Crystals Grown From PEG and Complexed With Crystallization Additives IV. Determined by X-ray diffraction at 1.18 Å resolution. Released 24 Sept 2025.

Method
X-ray diffraction
Resolution
1.18 Å
Organism
Sus scrofa
Chains
4
Atoms
8,920
Mol. weight
112.92 kDa
Ligands
BEN, PG5, PG6, CA
Released
24 Sept 2025

Explore 9PDA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PDA contains 36 α-helices and 76 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: 9 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand1711
β-strand20-2122
α-helix22-232
β-strand30-3453
β-strand38-4693
β-strand49-5243
α-helix54-563
β-strand62-6543
β-strand6914
β-strand78-87103
β-strand101-10553
α-helix108-1114
β-strand11912
α-helix120-1212
α-helix124-1263
β-strand130-13562
β-strand14914
β-strand151-15772
α-helix158-1592
α-helix160-1667
β-strand175-17842
β-strand18611
β-strand195-19842
β-strand201-20882
β-strand219-22352
α-helix224-2274
α-helix228-2369
Chain B: 10 helices, 22 β-strands
ElementResiduesLengthSheet
β-strand1715
β-strand20-2126
α-helix22-232
β-strand30-3457
β-strand38-4697
β-strand49-5247
α-helix54-563
β-strand62-6547
β-strand6918
β-strand78-87107
β-strand101-10557
α-helix108-1114
β-strand11219
β-strand11519
β-strand11916
α-helix120-1212
α-helix124-1263
β-strand130-13566
β-strand14918
α-helix1501
β-strand151-15776
α-helix158-1592
α-helix160-1667
β-strand175-17846
β-strand18615
β-strand195-19846
β-strand201-20886
β-strand214110
β-strand217110
β-strand219-22356
α-helix224-2263
α-helix228-23710
Chain D: 8 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand17115
β-strand20-21216
α-helix22-232
β-strand30-34517
β-strand38-46917
β-strand49-52417
α-helix54-563
β-strand62-65417
β-strand69118
β-strand78-871017
β-strand101-105517
β-strand119116
α-helix120-1212
α-helix124-1263
β-strand130-135616
β-strand149118
β-strand151-157716
α-helix158-1592
α-helix160-1667
β-strand175-178416
β-strand186115
β-strand195-198416
β-strand201-208816
β-strand219-223516
α-helix224-2263
α-helix228-23710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
TrypsinA, B, C, Dprotein231Sus scrofaP00761 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9PDA_1 Trypsin (chains A, B, C, D)
FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGE
HNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAA
GTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDS
CQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN

Ligands and cofactors

IDNameFormulaCopies
BENBenzamidineC7 H8 N210
PG51-methoxy-2-[2-(2-methoxy-ethoxy]-ethaneC8 H18 O412
PG61-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethaneC12 H26 O61
CACalcium ionCa5
MLIMalonate ionC3 H2 O44
PMAPyromellitic acidC10 H6 O82

Water and common crystallization additives (PEG, PG4, EPE, CL) are not listed.

Primary citation

X-ray Diffraction Analyses of Trypsin Crystals Grown in the Presence of Additives. McPherson, A. Cryst Growth Des (2026) 26:352-364. DOI 10.1021/acs.cgd.5c01305

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

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