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Crystal structure of the seca protein translocation ATPase from mycobacterium tuberculosis in apo form

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

PDB: 1NL3
Type: protein
Length: 1,677 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Preprotein translocase seca 1 subunit
UniProt: P0A5Y8
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Preprotein translocase seca 1 subunit	protein	839	56% helix, 10% strand	P0A5Y8
B	Preprotein translocase seca 1 subunit	protein	838	54% helix, 11% strand	P0A5Y8

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	549	0.79	0.86	63	empty
2	584	0.79	0.85	66	empty
3	869	0.76	0.80	102	empty
4	777	0.75	0.80	83	empty
5	282	0.70	0.84	44	empty

Interfaces

1 interface between chains.

A–B · 1387 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1NL3 · CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0A5Y8
Elsewhere: RCSB PDB 1NL3 · PDBe 1NL3 · UniProt P0A5Y8

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