1HJ9: Beta-trypsin

Atomic resolution structures of trypsin provide insight into structural radiation damage. Determined by X-ray diffraction at 0.95 Å resolution. Released 4 Jan 2002.

Method: X-ray diffraction
Resolution: 0.95 Å
Organism: BOS TAURUS
Chains: 1
Atoms: 1,965
Mol. weight: 23.84 kDa
Ligands: ANL, CA
Released: 4 Jan 2002

Explore 1HJ9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HJ9 contains 7 α-helices and 16 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: 7 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	20-21	2	1
β-strand	30-34	5	2
β-strand	40-48	9	2
β-strand	51-54	4	2
α-helix	56-58	3
β-strand	64-67	4	2
β-strand	81-90	10	2
β-strand	104-108	5	2
β-strand	115	1	3
β-strand	118	1	3
β-strand	122	1	1
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	1
β-strand	156-161	6	1
α-helix	162-164	3
α-helix	165-171	7
β-strand	180-182	3	1
β-strand	198-201	4	1
β-strand	204-215	8	1
β-strand	227-230	4	1
α-helix	231-234	4
α-helix	235-242	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-trypsin	A	protein	223	BOS TAURUS	P00760 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1HJ9_1 BETA-TRYPSIN (chains A)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAYGLEGKGDSCQGDSGGP
VVCSGKLQGIVSWGSGCQAKNKPGVYTKVCNYVSWIKQTIASN

Ligands and cofactors

ID	Name	Formula	Copies
ANL	Aniline	C6 H7 N	1
CA	Calcium ion	Ca	1

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

Primary citation

Atomic Resolution Structure of Trypsin Provide Insight Into Structural Radiation Damage. Leiros, H.-K.S., Mcsweeney, S.M., Smalas, A.O. Acta Crystallogr D Biol Crystallogr (2001) 57:488. DOI 10.1107/S0907444901000646 · 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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