3MFJ: Bovine trypsin

Bovine trypsin at 0.8 A resolution, restrained refinement. Determined by X-ray diffraction at 0.8 Å resolution. Released 21 Apr 2010.

Method: X-ray diffraction
Resolution: 0.8 Å
Organism: Bos taurus
Chains: 1
Atoms: 2,226
Mol. weight: 23.67 kDa
Ligands: CA, BEN
Released: 21 Apr 2010

Explore 3MFJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MFJ contains 6 α-helices and 20 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: 6 helices, 20 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
β-strand	115	1	4
β-strand	118	1	4
β-strand	122	1	2
α-helix	123-124	2
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	5
β-strand	224	1	5
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-244	10

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

>3MFJ_1 Cationic trypsin (chains A)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
BEN	Benzamidine	C7 H8 N2	1

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

Primary citation

Bovine trypsin at 0.8 A and role of restraints at ultra-high resolution. Brzuszkiewicz, A., Dauter, M., Dauter, Z. To be published.

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)
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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