5WI6: Human beta-1 tryptase mutant Ile99Cys

Human beta-1 tryptase mutant Ile99Cys. Determined by X-ray diffraction at 2.72 Å resolution. Released 25 Apr 2018.

Method: X-ray diffraction
Resolution: 2.72 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,828
Mol. weight: 112.12 kDa
Ligands: 0GJ
Released: 25 Apr 2018

Explore 5WI6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5WI6 contains 45 α-helices and 92 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: 11 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-35	6	3
β-strand	39-48	10	3
β-strand	51-54	4	3
α-helix	56-59	4
β-strand	60B	1	4
α-helix	61-63	3
β-strand	64-68	5	3
β-strand	72	1	5
β-strand	82-90	9	3
α-helix	97-99	3
β-strand	104-108	5	3
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-125	3
β-strand	135-140	6	2
β-strand	145	1	6
β-strand	149	1	6
α-helix	150-152	3
β-strand	154	1	5
β-strand	156-163	8	2
α-helix	165-173	9
β-strand	173C	1	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-203	6	2
β-strand	206-215	10	2
β-strand	221A	1	8
β-strand	224	1	8
α-helix	225	1
β-strand	226-230	5	2
α-helix	232-234	3
α-helix	235-239	5

Chain B: 12 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	9
β-strand	20-21	2	10
α-helix	22-23	2
β-strand	30-35	6	11
β-strand	39-48	10	11
β-strand	51-54	4	11
α-helix	56-59	4
β-strand	60B	1	12
α-helix	61-63	3
β-strand	64-68	5	11
β-strand	72	1	13
β-strand	82-90	9	11
α-helix	97-99	3
β-strand	104-108	5	11
α-helix	120-121	2
β-strand	122	1	10
α-helix	123-125	3
β-strand	135-140	6	10
β-strand	145	1	14
β-strand	149	1	14
α-helix	150-152	3
β-strand	154	1	13
α-helix	155	1
β-strand	156-163	8	10
α-helix	165-173	9
β-strand	173C	1	15
β-strand	180-183	4	10
β-strand	189	1	9
β-strand	198-203	6	10
β-strand	206-215	10	10
α-helix	225	1
β-strand	226-230	5	10
α-helix	232-234	3
α-helix	235-239	5

Chain C: 11 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	16
β-strand	20-21	2	17
α-helix	22-23	2
β-strand	30-35	6	18
β-strand	39-48	10	18
β-strand	51-54	4	18
α-helix	56-58	3
β-strand	60B	1	15
α-helix	61-63	3
β-strand	64-68	5	18
β-strand	72	1	19
β-strand	82-90	9	18
α-helix	97-99	3
β-strand	104-108	5	18
α-helix	120-121	2
β-strand	122	1	17
α-helix	123-125	3
β-strand	135-140	6	17
β-strand	145	1	20
β-strand	149	1	20
α-helix	150-152	3
β-strand	154	1	19
α-helix	155	1
β-strand	156-163	8	17
α-helix	165-173	9
β-strand	173C	1	12
β-strand	180-183	4	17
β-strand	189	1	16
β-strand	198-203	6	17
β-strand	206-215	10	17
β-strand	221A	1	21
β-strand	224	1	21
β-strand	226-230	5	17
α-helix	231-234	4
α-helix	235-239	5

Chain D: 11 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	22
β-strand	20-21	2	23
α-helix	22-23	2
β-strand	30-35	6	24
β-strand	39-48	10	24
β-strand	51-54	4	24
α-helix	56-58	3
β-strand	60B	1	7
α-helix	61-63	3
β-strand	64-68	5	24
β-strand	72	1	25
β-strand	82-90	9	24
α-helix	97-99	3
β-strand	104-108	5	24
α-helix	120-121	2
β-strand	122	1	23
α-helix	123-125	3
β-strand	135-140	6	23
β-strand	145	1	26
β-strand	149	1	26
α-helix	150-152	3
β-strand	154	1	25
α-helix	155	1
β-strand	156-163	8	23
α-helix	165-173	9
β-strand	173C	1	4
β-strand	180-183	4	23
β-strand	189	1	22
β-strand	198-203	6	23
β-strand	206-215	10	23
β-strand	226-230	5	23
α-helix	232-234	3
α-helix	235-239	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tryptase alpha/beta-1	A, B, C, D	protein	245	Homo sapiens	Q15661 (AlphaFold model)

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

>5WI6_1 Tryptase alpha/beta-1 (chains A, B, C, D)
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQL
REQHLYYQDQLLPVSRIIVHPQFYTAQCGADIALLELEEPVNVSSHVHTVTLPPASETFP
PGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDML
CAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPKKP

Ligands and cofactors

ID	Name	Formula	Copies
0GJ	L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydr…	C14 H28 Cl N6 O5	4

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

Primary citation

Dual functionality of beta-tryptase protomers as both proteases and cofactors in the active tetramer. Maun, H.R., Liu, P.S., Franke, Y. et al. J Biol Chem (2018) 293:9614-9628. DOI 10.1074/jbc.M117.812016 · PubMed

Other PDB entries of the same protein (UniProt Q15661 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2F9N 1.6 Å, Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant K192Q/D216G in…
4MPU 1.65 Å, Human beta-tryptase co-crystal structure with (6S,8R)-N,N'-bis[3-({4-[3-(aminomethyl)phen…
5F03 1.94 Å, TRYPTASE B2 IN COMPLEX WITH 5-(3-Aminomethyl-phenoxymethyl)-3-[3-(2-chloro-pyridin-3-ylet…
4MPW 1.95 Å, Human beta-tryptase co-crystal structure with [(1,1,3,3-tetramethyldisiloxane-1,3-diyl)di…
4MPX 2.0 Å, Human beta-tryptase co-crystal structure with [(1,1,3,3-tetramethyldisiloxane-1,3-diyl)di…
2ZEC 2.06 Å, Potent, Nonpeptide Inhibitors of Human Mast Cell Tryptase
2F9O 2.1 Å, Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G
6O1F 2.15 Å, Complex between soybean trypsin inhibitor beta1-tryptase and a humanized fab
1LTO 2.2 Å, Human alpha1-tryptase
4MQA 2.25 Å, Human beta-tryptase co-crystal structure with {(1,1,3,3-tetramethyldisiloxane-1,3-diyl)bi…
2F9P 2.3 Å, Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with…
4MPV 2.31 Å, Human beta-tryptase co-crystal structure with (2R,4S)-N,N'-bis[3-({4-[3-(aminomethyl)phen…

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