2F9P: Recombinant Human Alpha I Tryptase Mutant D216G

Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G in Complex with Leupeptin. Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Jan 2006.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Homo sapiens, Actinomycetes Streptomyces roseus MA 839-A1
Chains: 8
Atoms: 8,527
Mol. weight: 113.31 kDa
Ligands: BU3, NAG
Released: 31 Jan 2006

Explore 2F9P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F9P contains 40 α-helices and 106 β-strands across 8 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: 10 helices, 26 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
β-strand	104-108	5	3
α-helix	111-114	4
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	156-159	4	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	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	232-234	3
α-helix	235-238	4

Chains B and D: 10 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	56-58	3
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	83-90	8	11
β-strand	104-108	5	11
α-helix	111-114	4
β-strand	122	1	10
α-helix	123-125	3
β-strand	136-140	5	10
β-strand	145	1	14
β-strand	149	1	14
α-helix	150-152	3
β-strand	154	1	13
β-strand	156-160	5	10
β-strand	162-163	2	10
α-helix	165-171	7
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	235-238	4

Chain C: 10 helices, 26 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-60D	2
α-helix	61-63	3
β-strand	64-68	5	19
β-strand	72	1	20
β-strand	83	1	19
β-strand	85-90	6	19
β-strand	104-108	5	19
α-helix	111-114	4
β-strand	122	1	18
α-helix	123-125	3
β-strand	136-140	5	18
β-strand	145	1	21
β-strand	149	1	21
α-helix	150-152	3
β-strand	154	1	20
β-strand	156-159	4	18
β-strand	162-163	2	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	235-238	4

Chains E, F, G and H: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	303	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tryptase alpha-1	A, B, C, D	protein	245	Homo sapiens	Q15661 (AlphaFold model)
Leupeptin	E, F, G, H	protein	4	Actinomycetes Streptomyces roseus MA 839-A1

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

>2F9P_1 Tryptase alpha-1 (chains A, B, C, D)
IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLATLRVQL
REQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEPVNISSRVHTVMLPPASETFP
PGMPCWVTGWGDVDNDEPLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIIRDDML
CAGNSQRDSCKGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY
VPKKP

Sequence of entity 2 (E, F, G, H), FASTA

>2F9P_2 Leupeptin (chains E, F, G, H)
XLLR

Ligands and cofactors

ID	Name	Formula	Copies
BU3	(r,r)-2,3-butanediol	C4 H10 O2	4
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

X-ray Structures of Free and Leupeptin-complexed Human alpha I-Tryptase Mutants: Indication for an alpha to beta-Tryptase Transition. Rohr, K.B., Selwood, T., Marquardt, U. et al. J Mol Biol (2005) 357:195-209. DOI 10.1016/j.jmb.2005.12.037 · 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…
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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