4BNR: Hepatopancreas trypsin

Extremely stable complex of crayfish trypsin with bovine trypsin inhibitor. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Sept 2013.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: PONTASTACUS LEPTODACTYLUS, BOS TAURUS
Chains: 4
Atoms: 4,925
Mol. weight: 72.33 kDa
Ligands: CA
Released: 4 Sept 2013

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

Secondary structure: helices and β-sheets

4BNR contains 18 α-helices and 47 β-strands across 4 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: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
β-strand	30-37	8	3
β-strand	37C-48	12	3
β-strand	51-54	4	3
β-strand	64-68	5	3
β-strand	72	1	4
β-strand	81-90	10	3
β-strand	95	1	5
β-strand	100	1	5
β-strand	104-108	5	3
α-helix	111-114	4
β-strand	135-140	6	2
α-helix	149-152	3
β-strand	154	1	4
β-strand	156-163	8	2
α-helix	165-172	8
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-201	4	2
β-strand	208-215	8	2
β-strand	227-231	5	2
α-helix	232-234	3
α-helix	236-242	7

Chain B: 6 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	6
β-strand	20-21	2	7
β-strand	30-37	8	8
β-strand	37C-48	12	8
β-strand	51-54	4	8
β-strand	64-68	5	8
β-strand	72	1	9
β-strand	81-90	10	8
β-strand	95	1	10
β-strand	100	1	10
β-strand	104-108	5	8
α-helix	111-114	4
β-strand	122	1	7
α-helix	123-125	3
α-helix	128-130	3
β-strand	135-140	6	7
β-strand	154	1	9
β-strand	156-163	8	7
α-helix	165-172	8
β-strand	180-183	4	7
β-strand	189	1	6
β-strand	198-201	4	7
β-strand	208-215	8	7
β-strand	227-231	5	7
α-helix	232-234	3
α-helix	236-242	7

Chain I: 4 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
α-helix	8-9	2
β-strand	14	1	2
β-strand	18-24	7	11
β-strand	29-35	7	11
β-strand	45	1	11
α-helix	48-51	4
α-helix	52-56	5

Chain J: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
α-helix	8-9	2
β-strand	14	1	7
β-strand	18-24	7	12
β-strand	29-35	7	12
β-strand	45	1	12
α-helix	48-55	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hepatopancreas trypsin	A, B	protein	237	PONTASTACUS LEPTODACTYLUS	Q52V24 (AlphaFold model)
Pancreatic trypsin inhibitor	I, J	protein	100	BOS TAURUS	P00974 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4BNR_1 HEPATOPANCREAS TRYPSIN (chains A, B)
IVGGTDATLGEFPYQLSFQETFIGFSFHFCGASIYNENYAITAGHCVYGDDYENPSGLQI
VAGELDMSVNEGSEQIITVSKIILHENFDYNLLDNDISLLKLSGSLTFNDNVAPIALPEQ
GHTATGDVIVTGWGTTSEGGNTPDVLQKVTVPLVSDEDCRADYGADEILDSMICAGVPEG
GKDSCQGDSGGPLAASDTGSTYLAGIVSWGYGCARPGYPGVYTEVSYHVDWIKANAV

Sequence of entity 2 (I, J), FASTA

>4BNR_2 PANCREATIC TRYPSIN INHIBITOR (chains I, J)
MKMSRLCLSVALLVLLGTLAASTPGCDTSNQAKAQRPDFCLEPPYTGPCKARIIRYFYNA
KAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGAIGPWENL

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	4

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

Primary citation

Comparison of Complexes Formed by a Crustacean and a Vertebrate Trypsin with Bovine Pancreatic Trypsin Inhibitor - the Key to Achieving Extreme Stability? Molnar, T., Voros, J., Szeder, B. et al. FEBS J (2013) 280:5750. DOI 10.1111/FEBS.12491 · PubMed

Other PDB entries of the same protein (UniProt Q52V24 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2F91 1.2 Å, 1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI

Browse structure collections

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