5TNY: HTRA2 G399S mutant

HTRA2 G399S mutant. Determined by X-ray diffraction at 1.7 Å resolution. Released 25 Oct 2017.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,249
Mol. weight: 36.2 kDa
Released: 25 Oct 2017

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

Secondary structure: helices and β-sheets

5TNY contains 12 α-helices and 21 β-strands across 1 chain. 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: 12 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	144-147	4
α-helix	149-157	9
α-helix	158-160	3
β-strand	161-170	10	1
β-strand	175-188	14	1
β-strand	192-195	4	1
α-helix	197-200	4
β-strand	205-209	5	1
β-strand	215-224	10	1
β-strand	229-233	5	1
α-helix	239-241	3
β-strand	245	1	2
α-helix	248-250	3
α-helix	251-252	2
β-strand	256-259	4	2
β-strand	271-275	5	2
α-helix	294	1
β-strand	295-297	3	2
β-strand	309-311	3	2
β-strand	317-326	10	2
β-strand	329-334	6	2
α-helix	335-342	8
β-strand	360-361	2	3
β-strand	364-368	5	4
α-helix	371-380	10
β-strand	391-396	6	4
α-helix	401-405	5
β-strand	412-416	5	4
β-strand	420	1	4
α-helix	424-431	8
β-strand	437-441	5	4
β-strand	448-452	5	4
β-strand	455-456	2	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine protease HTRA2, mitochondrial	A	protein	332	Homo sapiens	O43464 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5TNY_1 Serine protease HTRA2, mitochondrial (chains A)
MAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGL
IVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVR
QGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVN
LDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPS
ILAELQLREPSFPDVQHGVLIHKVILSSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVR
TQSQLAVQIRRGRETLTLYVTPEVTEHHHHHH

Primary citation

Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2. Merski, M., Moreira, C., Abreu, R.M. et al. Cell Death Dis (2017) 8:e3119-e3119. DOI 10.1038/cddis.2017.487 · PubMed

Other PDB entries of the same protein (UniProt O43464 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5M3N 1.65 Å, HTRA2 wild-type structure
5TO1 1.69 Å, HtrA2 exposed (L266R, F303A) mutant
5M3O 1.7 Å, HTRA2 A141S mutant structure
5TNZ 1.75 Å, HtrA2 S142D mutant
5TO0 1.9 Å, HTRA2 S276C mutant
5FHT 1.95 Å, HtrA2 protease mutant V226K
1LCY 2.0 Å, Crystal Structure of the Mitochondrial Serine Protease HtrA2
5WYN 2.05 Å, HtrA2 Pathogenic Mutant
2PZD 2.75 Å, Crystal Structure of the HtrA2/Omi PDZ Domain Bound to a Phage-Derived Ligand (WTMFWV)
8E2K 3.21 Å, Cryo-EM structure of BIRC6/HtrA2-S306A
7VGE 4.0 Å, Structure of the PDZ deleted variant of HtrA2 protease (S306A)
8AUK 6.2 Å, Cryo-EM structure of human BIRC6 in complex with HTRA2.

Browse structure collections

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