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Crystal structure of the accessory translocation ATPase, SECA2, from mycobacterium tuberculosis

Analyse Crystal structure of the accessory translocation ATPase, SECA2, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UAQ
Type: protein
Length: 705 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein translocase subunit seca 2
UniProt: P9WGP3
Pockets: 9 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein translocase subunit seca 2	protein	705	49% helix, 12% strand	P9WGP3

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1015	0.78	0.80	111	empty
2	213	0.52	0.77	29	empty
3	172	0.52	0.78	24	empty
4	159	0.51	0.79	26	empty
5	103	0.50	0.81	21	empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

4UAQ · Crystal structure of the accessory translocation ATPase, SecA2, from Mycobacterium… · the same entry in another collection · chain A against A, TM-score 1.00
P9WGP3 · AlphaFold monomer V2.0 prediction for protein translocase subunit seca 2 (P9WGP3) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 P9WGP3
Elsewhere: RCSB PDB 4UAQ · PDBe 4UAQ · UniProt P9WGP3

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