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Crystal Structure of LpqW

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

PDB: 2GRV
Type: protein
Length: 1,536 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.4
Source: Mycobacterium smegmatis str. MC2 155
Molecule: LpqW
UniProt: Q1TT16
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · resolution 2.4 · 3 distinct chains · 29% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LpqW	protein	516	29% helix, 26% strand	Q1TT16
B	LpqW	protein	509	29% helix, 26% strand	Q1TT16
C	LpqW	protein	511	30% helix, 26% strand	Q1TT16

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	224	0.83	0.96	38	empty
2	227	0.81	0.95	36	empty
3	447	0.77	0.86	71	empty
4	847	0.76	0.80	89	empty
5	233	0.61	0.81	25	empty

Interfaces

1 interface between chains.

A–C · 1046 Å² buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2GRV · Crystal structure of lpqw · 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 Q1TT16
Elsewhere: RCSB PDB 2GRV · PDBe 2GRV · UniProt Q1TT16

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