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Crystal structure of HTRA1 from mycobacterium tuberculosis

Analyse Crystal structure of HTRA1 from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZVJ
Type: protein
Length: 299 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine protease
EC: 3.4.21.-, 3.4.21.107
UniProt: A0A1K3KH35
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine protease (EC 3.4.21.-, 3.4.21.107)	protein	299	17% helix, 39% strand	A0A1K3KH35

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.49	0.81	18	TRS
2	132	0.44	0.76	19	empty
3	88	0.32	0.73	15	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

5ZVJ · Crystal structure of HtrA1 from Mycobacterium tuberculosis · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A1K3KH35
Elsewhere: RCSB PDB 5ZVJ · PDBe 5ZVJ · UniProt A0A1K3KH35

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