5MN1: Cationic trypsin

Cationic trypsin in complex with 2-aminopyridine (deuterated sample at 100 K). Determined by X-ray diffraction at 0.79 Å resolution. Released 24 May 2017.

Method: X-ray diffraction
Resolution: 0.79 Å
Organism: Bos taurus
Chains: 1
Atoms: 2,522
Mol. weight: 23.84 kDa
Ligands: 2AP, CA
Released: 24 May 2017

Explore 5MN1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MN1 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

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	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	163-164	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	221A	1	4
β-strand	224	1	4
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-243	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cationic trypsin	A	protein	223	Bos taurus	P00760 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5MN1_1 Cationic trypsin (chains A)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Ligands and cofactors

ID	Name	Formula	Copies
2AP	2-aminopyridine	C5 H7 N2	1
CA	Calcium ion	Ca	1

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

Primary citation

Charges Shift Protonation: Neutron Diffraction Reveals that Aniline and 2-Aminopyridine Become Protonated Upon Binding to Trypsin. Schiebel, J., Gaspari, R., Sandner, A. et al. Angew Chem Int Ed Engl (2017) 56:4887-4890. DOI 10.1002/anie.201701038 · 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
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)
5MNC 0.92 Å, Cationic trypsin in complex with aniline (deuterated sample at 100 K)

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