4I8H: Bovine trypsin at 0.75 resolution

Bovine trypsin at 0.75 resolution. Determined by X-ray diffraction at 0.75 Å resolution. Released 19 Dec 2012.

Method: X-ray diffraction
Resolution: 0.75 Å
Organism: Bos taurus
Chains: 1
Atoms: 2,396
Mol. weight: 23.77 kDa
Ligands: BEN, CA
Released: 19 Dec 2012

Explore 4I8H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4I8H contains 6 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: 6 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
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	4
β-strand	224	1	4
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

>4I8H_1 Cationic trypsin (chains A)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Ligands and cofactors

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

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

Primary citation

On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin. Liebschner, D., Dauter, M., Brzuszkiewicz, A. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:1447-1462. DOI 10.1107/S0907444913009050 · PubMed

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

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)
5MNC 0.92 Å, Cationic trypsin in complex with aniline (deuterated sample at 100 K)

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