1A0L: Beta-tryptase

Human beta-tryptase: a ring-like tetramer with active sites facing a central pore. Determined by X-ray diffraction at 3.0 Å resolution. Released 23 Mar 1999.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,872
Mol. weight: 110.41 kDa
Ligands: APA
Released: 23 Mar 1999

Explore 1A0L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1A0L contains 37 α-helices and 109 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: 9 helices, 28 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	61-63	3
β-strand	64-67	4	3
β-strand	72	1	5
β-strand	83	1	3
β-strand	85-90	6	3
β-strand	104-108	5	3
β-strand	122	1	2
α-helix	123-125	3
β-strand	136-140	5	2
β-strand	145	1	6
β-strand	149	1	6
α-helix	150-152	3
β-strand	154	1	5
β-strand	156-160	5	2
β-strand	162-163	2	2
α-helix	165-173	9
β-strand	173C	1	7
β-strand	180-183	4	2
β-strand	185	1	8
β-strand	188	1	8
β-strand	189	1	1
β-strand	198-203	6	2
β-strand	206-215	10	2
β-strand	221A	1	9
β-strand	224	1	9
α-helix	225	1
β-strand	226-230	5	2
α-helix	232-234	3
α-helix	235-241	7

Chain B: 7 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	10
β-strand	20-21	2	11
α-helix	22-23	2
β-strand	30-36	7	12
β-strand	38-48	11	12
β-strand	51-54	4	12
α-helix	56-59	4
β-strand	60B	1	13
α-helix	61-63	3
β-strand	64-68	5	12
β-strand	72	1	14
β-strand	82-83	2	12
β-strand	85-90	6	12
β-strand	104-108	5	12
β-strand	122	1	11
α-helix	123-125	3
β-strand	136-140	5	11
β-strand	145	1	15
β-strand	149	1	15
β-strand	154	1	14
β-strand	156-160	5	11
β-strand	162-163	2	11
α-helix	165-171	7
β-strand	173C	1	16
β-strand	180-183	4	11
β-strand	185	1	17
β-strand	188	1	17
β-strand	189	1	10
β-strand	198-203	6	11
β-strand	206-215	10	11
β-strand	221A	1	18
β-strand	224	1	18
α-helix	225	1
β-strand	226-230	5	11
α-helix	231-241	11

Chain C: 9 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	19
β-strand	20-21	2	20
α-helix	22-23	2
β-strand	30-36	7	21
β-strand	38-48	11	21
β-strand	51-54	4	21
α-helix	56-59	4
β-strand	60B	1	16
α-helix	60C-60E	3
α-helix	61-63	3
β-strand	64-68	5	21
β-strand	72	1	22
β-strand	82-90	9	21
β-strand	104-108	5	21
α-helix	120-121	2
β-strand	122	1	20
α-helix	123-125	3
β-strand	136-140	5	20
β-strand	145	1	23
β-strand	149	1	23
β-strand	154	1	22
β-strand	156-160	5	20
β-strand	162-163	2	20
α-helix	165-173	9
β-strand	173C	1	13
β-strand	180-183	4	20
β-strand	189	1	19
β-strand	198-203	6	20
β-strand	206-215	10	20
β-strand	221A	1	24
β-strand	224	1	24
β-strand	226-230	5	20
α-helix	232-234	3
α-helix	235-239	5

Chain D: 12 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	25
β-strand	20-21	2	26
α-helix	22-23	2
β-strand	30-36	7	27
β-strand	38-48	11	27
β-strand	51-54	4	27
α-helix	56-58	3
β-strand	60B	1	7
α-helix	60C-60E	3
α-helix	61-63	3
β-strand	64-68	5	27
β-strand	72	1	28
β-strand	83	1	27
β-strand	85-90	6	27
α-helix	97-99	3
β-strand	104-108	5	27
α-helix	120-121	2
β-strand	122	1	26
α-helix	123-125	3
β-strand	136-140	5	26
β-strand	145	1	29
β-strand	149	1	29
β-strand	154	1	28
α-helix	155	1
β-strand	156-160	5	26
β-strand	162-163	2	26
α-helix	165-171	7
β-strand	173C	1	4
β-strand	180-183	4	26
β-strand	185	1	30
β-strand	188	1	30
β-strand	189	1	25
β-strand	198-203	6	26
β-strand	206-215	10	26
β-strand	221A	1	31
β-strand	224	1	31
α-helix	225	1
β-strand	226-230	5	26
α-helix	231-234	4
α-helix	235-241	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-tryptase	A, B, C, D	protein	244	Homo sapiens	P20231 (AlphaFold model)

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

>1A0L_1 BETA-TRYPTASE (chains A, B, C, D)
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQL
REQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVKVSSHVHTVTLPPASETFP
PGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDML
CAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPKK

Ligands and cofactors

ID	Name	Formula	Copies
APA	(2S)-3-(4-carbamimidoylphenyl)-2-hydroxypropanoic acid	C10 H12 N2 O3	4

Primary citation

Human beta-tryptase is a ring-like tetramer with active sites facing a central pore. Pereira, P.J., Bergner, A., Macedo-Ribeiro, S. et al. Nature (1998) 392:306-311. DOI 10.1038/32703 · PubMed

Other PDB entries of the same protein (UniProt P20231 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9QFU 1.98 Å, Human Tryptase beta-2 (hTPSB2) complexed with covalent inhibitor Compound #1
2FPZ 2.0 Å, Human tryptase with 2-amino benzimidazole
4A6L 2.05 Å, beta-tryptase inhibitor
9QFV 2.06 Å, Human Tryptase beta-2 (hTPSB2)
3V7T 2.09 Å, Crystal Structure of Human Beta-Tryptase Complexed with a Synthetic Inhibitor with a…
2BM2 2.2 Å, human beta-II tryptase in complex with 4-(3-Aminomethyl-phenyl)-…
2FWW 2.25 Å, human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme
2FS9 2.3 Å, Human beta tryptase II with inhibitor CRA-28427
2ZA5 2.3 Å, Crystal Structure of human tryptase with potent non-peptide inhibitor
2GDD 2.35 Å, Human beta II tryptase with inhibitor CRA-27592
2FS8 2.5 Å, Human beta-tryptase II with inhibitor CRA-29382
2FXR 2.5 Å, human beta tryptase II complexed with activated ketone inhibitor CRA-29382

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