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Staphylococcus epidermidis tcar in complex with salicylate

Analyse Staphylococcus epidermidis tcar in complex with salicylate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KP6
Type: protein
Length: 276 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator tcar
UniProt: Q5HLN6
Ligands: SAL
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional regulator tcar	protein	139	67% helix, 3% strand	Q5HLN6
B	Transcriptional regulator tcar	protein	137	76% helix, 6% strand	Q5HLN6

Ligands and binding sites

SAL · 2-hydroxybenzoic acid · ligand · 8 copies · chains A, B
CAC · Cacodylate ion · additive · chains 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1090	0.81	0.82	91	SAL
2	302	0.78	0.88	31	SAL
3	82	0.51	0.84	16	SAL

Interfaces

1 interface between chains.

A–B · 2766 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

3KP6 · Staphylococcus epidermidis TcaR in complex with salicylate · 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 Q5HLN6
Elsewhere: RCSB PDB 3KP6 · PDBe 3KP6 · UniProt Q5HLN6

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