4HGC: Bovine trypsin

Crystal structure of bovine trypsin complexed with sfti-1 analog containing a peptoid residue at position p1. Determined by X-ray diffraction at 1.29 Å resolution. Released 9 Oct 2013.

Method: X-ray diffraction
Resolution: 1.29 Å
Organisms: Bos taurus, Helianthus annuus
Chains: 2
Atoms: 2,093
Mol. weight: 25.65 kDa
Ligands: CA
Released: 9 Oct 2013

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

Secondary structure: helices and β-sheets

4HGC contains 7 α-helices and 19 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, 17 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
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	216-217	2	4
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-243	9

Chain I: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	2-3	2	4
β-strand	11	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cationic trypsin	A	protein	223	Bos taurus	P00760 (AlphaFold model)
Trypsin inhibitor 1	I	protein	14	Helianthus annuus	Q4GWU5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4HGC_1 Cationic trypsin (chains A)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Sequence of entity 2 (I), FASTA

>4HGC_2 Trypsin inhibitor 1 (chains I)
GRCTXSIPPICFPD

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

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

Primary citation

Structure of a proteolytically resistant analogue of (NLys)(5)SFTI-1 in complex with trypsin: evidence for the direct participation of the Ser214 carbonyl group in serine protease-mediated proteolysis. Krzywda, S., Jaskolski, M., Rolka, K. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:668-675. DOI 10.1107/S1399004713032252 · 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)

Browse structure collections

About this viewer

MolViewer shows 4HGC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.