7JR1: Cationic trypsin

Crystal structure of the R64F mutant of Bauhinia Bauhinioides Kallikrein Inhibitor complexed with Bovine Trypsin. Determined by X-ray diffraction at 2.05 Å resolution. Released 21 Jul 2021.

Method: X-ray diffraction
Resolution: 2.05 Å
Organisms: Bos taurus, Bauhinia bauhinioides
Chains: 12
Atoms: 18,035
Mol. weight: 248.89 kDa
Released: 21 Jul 2021

Explore 7JR1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7JR1 contains 74 α-helices and 246 β-strands across 12 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: 8 helices, 22 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	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	115	1	6
β-strand	118	1	6
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	2
β-strand	154	1	4
β-strand	156-162	7	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	235-244	10

Chain B: 9 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	11
β-strand	20-21	2	12
β-strand	30-34	5	13
β-strand	40-48	9	13
β-strand	51-54	4	13
α-helix	56-58	3
α-helix	63	1
β-strand	64-67	4	13
β-strand	72	1	14
β-strand	81-90	10	13
β-strand	104-108	5	13
α-helix	111-114	4
β-strand	122	1	12
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	12
β-strand	154	1	14
β-strand	156-162	7	12
α-helix	163-164	2
α-helix	165-169	5
β-strand	180-183	4	12
β-strand	189	1	11
β-strand	198-201	4	12
β-strand	204-215	8	12
β-strand	221A	1	15
β-strand	224	1	15
β-strand	226-230	5	12
α-helix	231-234	4
α-helix	235-244	10

Chain C: 7 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	16
β-strand	20-21	2	17
β-strand	30-34	5	18
β-strand	40-48	9	18
β-strand	51-54	4	18
α-helix	56-58	3
β-strand	64-67	4	18
β-strand	72	1	19
β-strand	81-90	10	18
β-strand	95	1	20
β-strand	100	1	20
β-strand	104-108	5	18
β-strand	115	1	21
β-strand	118	1	21
α-helix	120-121	2
β-strand	122	1	17
α-helix	123-124	2
β-strand	135-140	6	17
β-strand	154	1	19
β-strand	156-162	7	17
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	17
β-strand	189	1	16
β-strand	198-201	4	17
β-strand	204-215	8	17
β-strand	226-230	5	17
α-helix	231-234	4
α-helix	235-244	10

Chain D: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	22
β-strand	20-21	2	23
β-strand	30-34	5	24
β-strand	40-48	9	24
β-strand	51-54	4	24
α-helix	56-58	3
α-helix	63	1
β-strand	64-67	4	24
β-strand	72	1	25
β-strand	81-90	10	24
β-strand	104-108	5	24
β-strand	115	1	26
β-strand	118	1	26
α-helix	120-121	2
β-strand	122	1	23
α-helix	123-124	2
α-helix	128-130	3
β-strand	135-140	6	23
β-strand	154	1	25
β-strand	156-162	7	23
α-helix	163	1
α-helix	165-171	7
β-strand	180-183	4	23
β-strand	189	1	22
β-strand	198-201	4	23
β-strand	204-215	8	23
β-strand	221A	1	27
β-strand	224	1	27
β-strand	226-230	5	23
α-helix	231-234	4
α-helix	235-244	10

Chain E: 8 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	28
β-strand	20-21	2	29
β-strand	30-34	5	30
β-strand	40-48	9	30
β-strand	51-54	4	30
α-helix	56-58	3
α-helix	63	1
β-strand	64-67	4	30
β-strand	81-90	10	30
β-strand	104-108	5	30
α-helix	111-114	4
β-strand	115	1	31
β-strand	118	1	31
β-strand	122	1	29
α-helix	123-124	2
β-strand	135-140	6	29
β-strand	156-162	7	29
α-helix	163-164	2
α-helix	165-171	7
β-strand	180-183	4	29
β-strand	189	1	28
β-strand	198-201	4	29
β-strand	204-215	8	29
β-strand	221A	1	32
β-strand	224	1	32
β-strand	226-230	5	29
α-helix	231-233	3
α-helix	235-244	10

Chain F: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	33
β-strand	20-21	2	34
β-strand	30-34	5	35
β-strand	40-48	9	35
β-strand	51-54	4	35
α-helix	56-58	3
β-strand	64-67	4	35
β-strand	72	1	36
β-strand	81-90	10	35
β-strand	95	1	37
β-strand	100	1	37
β-strand	104-108	5	35
α-helix	111-114	4
β-strand	115	1	38
β-strand	118	1	38
β-strand	122	1	34
α-helix	123-124	2
β-strand	135-140	6	34
β-strand	154	1	36
β-strand	156-163	8	34
α-helix	165-171	7
β-strand	180-183	4	34
β-strand	189	1	33
β-strand	198-201	4	34
β-strand	204-215	8	34
β-strand	226-230	5	34
α-helix	231-234	4
α-helix	235-243	9

Chain G: 6 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	2	1
β-strand	3	1	7
α-helix	4	1
β-strand	5	1	8
α-helix	10	1
β-strand	11	1	8
α-helix	12-13	2
β-strand	19-23	5	9
β-strand	30-34	5	9
β-strand	44-48	5	9
β-strand	52-53	2	10
β-strand	57-60	4	9
β-strand	63	1	2
β-strand	69	1	7
β-strand	74-78	5	9
β-strand	87-93	7	9
β-strand	97-103	7	9
β-strand	112-117	6	9
β-strand	120-125	6	9
α-helix	132-133	2
β-strand	134-141	8	9
β-strand	144-149	6	9
α-helix	154-156	3
β-strand	157-161	5	9

Chain H: 3 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	2	1
β-strand	3	1	39
α-helix	4	1
β-strand	5	1	40
β-strand	11	1	40
α-helix	12	1
β-strand	13	1	41
β-strand	19-23	5	42
β-strand	30-34	5	43
β-strand	44-48	5	43
β-strand	51-52	2	10
β-strand	57	1	42
β-strand	58-60	3	43
β-strand	63	1	12
β-strand	67	1	41
β-strand	69	1	39
β-strand	74	1	42
β-strand	75-77	3	43
β-strand	87-93	7	43
β-strand	97-103	7	43
β-strand	112-117	6	42
β-strand	120-125	6	42
β-strand	134-135	2	42
β-strand	136-141	6	43
β-strand	144-149	6	43
β-strand	157-161	5	42

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cationic trypsin	A, B, C, D, E, F	protein	223	Bos taurus	P00760 (AlphaFold model)
Kunitz-type inihibitor	G, H, I, J, K, L	protein	164	Bauhinia bauhinioides	P83052 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>7JR1_1 Cationic trypsin (chains A, B, C, D, E, F)
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG
NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG
WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP
VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

Sequence of entity 2 (G, H, I, J, K, L), FASTA

>7JR1_2 Kunitz-type inihibitor (chains G, H, I, J, K, L)
GSSVVVDTNGQPVSNGADAYYLVPVSHGHAGLALAKIGNEAEPRAVVLDPHHRPGLPVRF
ESPLFINIIKESYFLNIKFGPSSSDSGVWDVIQQDPIGLAVKVTDTKSLLGPFKVEKEGE
GYKIVYYPERGQTGLDIGLVHRNDKYYLAVKDGEPCVFKIRKAT

Primary citation

Structural studies of complexes of kallikrein 4 with wild-type and mutated forms of the Kunitz-type inhibitor BbKI. Li, M., Srp, J., Mares, M. et al. Acta Crystallogr D Struct Biol (2021) 77:1084-1098. DOI 10.1107/S2059798321006483 · 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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