1LTO: Human alpha1-tryptase

Human alpha1-tryptase. Determined by X-ray diffraction at 2.2 Å resolution. Released 20 May 2003.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,343
Mol. weight: 110.93 kDa
Released: 20 May 2003

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

Secondary structure: helices and β-sheets

1LTO contains 41 α-helices and 102 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, 25 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-36	7	3
β-strand	38-48	11	3
β-strand	51-54	4	3
α-helix	56-59	4
β-strand	60B	1	4
α-helix	60C-60E	3
α-helix	61-63	3
β-strand	64-68	5	3
β-strand	72	1	5
β-strand	83	1	3
β-strand	85-90	6	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	156-162	7	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
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-241	7

Chain B: 11 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	9
β-strand	20-21	2	10
α-helix	22-23	2
β-strand	30-36	7	11
β-strand	38-48	11	11
β-strand	51-54	4	11
α-helix	56-59	4
β-strand	60B	1	12
α-helix	60C-60E	3
α-helix	61-63	3
β-strand	64-67	4	11
β-strand	72	1	13
β-strand	83	1	11
β-strand	85-90	6	11
α-helix	97-99	3
β-strand	104-108	5	11
α-helix	111-114	4
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
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
β-strand	221A	1	16
β-strand	224	1	16
β-strand	226-230	5	10
α-helix	231-234	4
α-helix	235-241	7

Chain C: 10 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	17
β-strand	20-21	2	18
α-helix	22-23	2
β-strand	30-36	7	19
β-strand	38-48	11	19
β-strand	51-54	4	19
α-helix	56-59	4
β-strand	60B	1	15
α-helix	60C-60E	3
α-helix	61-63	3
β-strand	64-67	4	19
β-strand	72	1	20
β-strand	83-90	8	19
α-helix	97-99	3
β-strand	104-108	5	19
β-strand	122	1	18
α-helix	123-125	3
β-strand	135-140	6	18
β-strand	145	1	21
β-strand	149	1	21
α-helix	150-152	3
β-strand	154	1	20
β-strand	156-162	7	18
α-helix	165-173	9
β-strand	173C	1	12
β-strand	180-183	4	18
β-strand	189	1	17
β-strand	198-203	6	18
β-strand	206-215	10	18
β-strand	221A	1	22
β-strand	224	1	22
β-strand	226-230	5	18
α-helix	231-234	4
α-helix	235-239	5

Chain D: 9 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	23
β-strand	20-21	2	24
α-helix	22-23	2
β-strand	30-36	7	25
β-strand	38-48	11	25
β-strand	51-54	4	25
α-helix	56-59	4
β-strand	60B	1	7
α-helix	60C-60E	3
α-helix	61-63	3
β-strand	64-67	4	25
β-strand	72	1	26
β-strand	83	1	25
β-strand	85-90	6	25
α-helix	97-99	3
β-strand	104-108	5	25
β-strand	115	1	27
β-strand	118	1	27
β-strand	122	1	24
α-helix	123-125	3
β-strand	136-140	5	24
β-strand	145	1	28
β-strand	149	1	28
α-helix	150-152	3
β-strand	154	1	26
β-strand	156-159	4	24
β-strand	162-163	2	24
α-helix	165-173	9
β-strand	173C	1	4
β-strand	180-183	4	24
β-strand	189	1	23
β-strand	198-203	6	24
β-strand	206-215	10	24
β-strand	221A	1	29
β-strand	224	1	29
β-strand	226-230	5	24
α-helix	231-238	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
alpha tryptase I	A, B, C, D	protein	245	Homo sapiens	Q15661 (AlphaFold model)

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

>1LTO_1 alpha tryptase I (chains A, B, C, D)
IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCLGPDVKDLATLRVQL
REQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEPVNISSRVHTVMLPPASETFP
PGMPCWVTGWGDVDNDEPLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIIRDDML
CAGNSQRDSCKGDSGGPLVCKVNGTWLQAGVVSWDEGCAQPNRPGIYTRVTYYLDWIHHY
VPKKP

Primary citation

The Crystal Structure of Human alpha1-Tryptase Reveals a Blocked Substrate-binding Region. Marquardt, U., Zettl, F., Huber, R. et al. J Mol Biol (2002) 321:491-502. DOI 10.1016/S0022-2836(02)00625-3 · 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
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…
8VGK 2.4 Å, CryoEM structure of tryptase in complex with engineered conformationally rigid…

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