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Structural basis for tetm-mediated tetracycline resistance

Analyse Structural basis for tetm-mediated tetracycline resistance in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3J25
Type: protein
Length: 638 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tetracycline resistance protein tetm
UniProt: Q47810
Ligands: GCP
Pockets: 7 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 29% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tetracycline resistance protein tetm	protein	638	29% helix, 8% strand	Q47810

Ligands and binding sites

GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A

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

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1186	0.80	0.82	140	empty
2	1009	0.77	0.80	102	empty
3	533	0.72	0.81	60	empty
4	672	0.67	0.76	73	empty
5	585	0.66	0.77	65	empty

Compared structures

3J25 · Structural basis for TetM-mediated tetracycline resistance · the same entry in another collection · chain A against A, TM-score 1.00
Q47810 · AlphaFold monomer V2.0 prediction for tetracycline resistance protein tetm from… · a predicted model of the same protein · chain A against A, TM-score 0.70

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 Q47810
Elsewhere: RCSB PDB 3J25 · PDBe 3J25 · UniProt Q47810

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