7PH1: Trypsin

Trypsin in complex with BPTI mutant (2S)-2-amino-4-monofluorobutanoic acid. Determined by X-ray diffraction at 1.18 Å resolution. Released 30 Mar 2022.

Method: X-ray diffraction
Resolution: 1.18 Å
Organism: Bos taurus
Chains: 2
Atoms: 2,794
Mol. weight: 31.79 kDa
Ligands: CA
Released: 30 Mar 2022

Explore 7PH1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7PH1 contains 10 α-helices and 22 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 E: 7 helices, 18 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	111-114	4
β-strand	115	1	4
β-strand	118	1	4
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	191	1	1
β-strand	200-203	4	2
β-strand	206-213	8	2
β-strand	224-228	5	2
α-helix	229-232	4
α-helix	233-241	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	5
β-strand	29-35	7	5
β-strand	45	1	5
α-helix	48-55	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cationic trypsin	E	protein	223	Bos taurus	P00760 (AlphaFold model)
Pancreatic trypsin inhibitor	I	protein	57	Bos taurus	P00974 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>7PH1_1 Cationic trypsin (chains E)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Sequence of entity 2 (I), FASTA

>7PH1_2 Pancreatic trypsin inhibitor (chains I)
PDFCLEPPYTGPCXARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

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

Primary citation

Water Network in the Binding Pocket of Fluorinated BPTI-Trypsin Complexes─Insights from Simulation and Experiment. Wehrhan, L., Leppkes, J., Dimos, N. et al. J Phys Chem B (2022) 126:9985-9999. DOI 10.1021/acs.jpcb.2c05496 · 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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