1P2J: Trypsinogen, cationic

Structural consequences of accommodation of four non-cognate amino-acid residues in the S1 pocket of bovine trypsin and chymotrypsin. Determined by X-ray diffraction at 1.35 Å resolution. Released 20 Apr 2004.

Method: X-ray diffraction
Resolution: 1.35 Å
Organism: Bos taurus
Chains: 2
Atoms: 2,347
Mol. weight: 30.24 kDa
Ligands: CA
Released: 20 Apr 2004

Explore 1P2J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1P2J contains 10 α-helices and 20 β-strands across 2 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 A: 7 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
β-strand	30-34	5	3
β-strand	40-48	9	3
β-strand	51-54	4	3
α-helix	56-58	3
β-strand	64-67	4	3
β-strand	81-90	10	3
β-strand	104-108	5	3
α-helix	111-113	3
β-strand	122	1	2
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	2
β-strand	156-162	7	2
α-helix	165-171	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	204-215	8	2
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-243	9

Chain I: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	8-9	2
β-strand	14	1	2
β-strand	18-24	7	4
β-strand	29-35	7	4
β-strand	45	1	4
α-helix	48-55	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Trypsinogen, cationic	A	protein	223	Bos taurus	P00760 (AlphaFold model)
Pancreatic trypsin inhibitor	I	protein	58	Bos taurus	P00974 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1P2J_1 Trypsinogen, cationic (chains A)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Sequence of entity 2 (I), FASTA

>1P2J_2 Pancreatic trypsin inhibitor (chains I)
RPDFCLEPPYTGPCLARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCLRTCGGA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

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

Primary citation

Structural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin. Helland, R., Czapinska, H., Leiros, I. et al. J Mol Biol (2003) 333:845-861. DOI 10.1016/j.jmb.2003.08.059 · PubMed

Other PDB entries of the same protein (UniProt P00760 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4I8H 0.75 Å, Bovine trypsin at 0.75 resolution
5MN1 0.79 Å, Cationic trypsin in complex with 2-aminopyridine (deuterated sample at 100 K)
5MNK 0.8 Å, Cationic trypsin in complex with benzylamine (deuterated sample at 100 K)
3MFJ 0.8 Å, Bovine trypsin at 0.8 A resolution, restrained refinement
3MI4 0.8 Å, Bovine trypsin at 0.8 A resolution, non-restrained refinement
4I8G 0.8 Å, Bovine trypsin at 0.8 resolution
4I8K 0.85 Å, Bovine trypsin at 0.85 resolution
5MNN 0.86 Å, Cationic trypsin in complex with N-amidinopiperidine (deuterated sample at 100 K)
5MNG 0.86 Å, Cationic trypsin in complex with benzamidine (deuterated sample at 100 K)
4I8J 0.87 Å, Bovine trypsin at 0.87 A resolution
4I8L 0.87 Å, Bovine trypsin at 0.87 resolution
4XOJ 0.91 Å, Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)

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