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Structure of smet, the repressor of the stenotrophomonas maltophilia multidrug efflux pump smedef.

Analyse Structure of smet, the repressor of the stenotrophomonas maltophilia multidrug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W53
Type: protein
Length: 375 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Repressor
UniProt: Q8KLP4
Ligands: SO4
Pockets: 3 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Repressor	protein	202	70% helix, 1% strand	Q8KLP4
B	Repressor	protein	173	71% helix, 1% strand	Q8KLP4

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	206	0.85	0.97	23	empty
2	300	0.83	0.93	40	empty
3	82	0.30	0.72	19	empty

Interfaces

1 interface between chains.

A–B · 1318 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2W53 · Structure of SmeT, the repressor of the Stenotrophomonas maltophilia multidrug efflux… · 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 Q8KLP4
Elsewhere: RCSB PDB 2W53 · PDBe 2W53 · UniProt Q8KLP4

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