2PTC: Beta-trypsin

The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Determined by X-ray diffraction at 1.9 Å resolution. Released 18 Jan 1983.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Bos taurus
Chains: 2
Atoms: 2,241
Mol. weight: 29.89 kDa
Ligands: CA
Released: 18 Jan 1983

Explore 2PTC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PTC contains 11 α-helices and 20 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 E: 8 helices, 16 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	226-230	5	2
α-helix	231-234	4
α-helix	235-243	9

Chain I: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	8-9	2
β-strand	14	1	2
β-strand	18-24	7	4
β-strand	29-35	7	4
β-strand	45	1	4
α-helix	48-55	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-trypsin	E	protein	223	Bos taurus	P00760 (AlphaFold model)
Trypsin inhibitor	I	protein	58		P00974 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>2PTC_1 BETA-TRYPSIN (chains E)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Sequence of entity 2 (I), FASTA

>2PTC_2 TRYPSIN INHIBITOR (chains I)
RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGA

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1

Primary citation

The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors. Marquart, M., Walter, J., Deisenhofer, J. et al. Acta Crystallogr B (1983) 39:480. 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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