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TETR(D) T103A mutant in complex with anhydrotetracycline and magnesium, I4(1)22

Analyse TETR(D) T103A mutant in complex with anhydrotetracycline and magnesium, I4(1)22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FKM
Type: protein
Length: 203 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetracycline repressor, class D
UniProt: C6G9U5
Ligands: TDC, MG, CL
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetracycline repressor, class D	protein	203	73% helix, 0% strand	C6G9U5

Ligands and binding sites

TDC · 5A,6-anhydrotetracycline · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 4 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	269	0.65	0.82	32	TDC, MG
2	50	0.33	0.78	11	empty

Compared structures

5FKM · TetR(D) T103A mutant in complex with anhydrotetracycline and magnesium, I4(1)22 · 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 C6G9U5
Elsewhere: RCSB PDB 5FKM · PDBe 5FKM · UniProt C6G9U5

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