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Crystal structure of tetr-family transcriptional regulator from streptomyces coelicolor

Analyse Crystal structure of tetr-family transcriptional regulator from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3BNI
Type
protein
Length
345 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative tetr-family transcriptional regulator
UniProt
Q8CK21
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative tetr-family transcriptional regulatorprotein17477% helix, 0% strandQ8CK21
BPutative tetr-family transcriptional regulatorprotein17177% helix, 0% strandQ8CK21

Ligands and binding sites

  • PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11890.740.9029PG4
22210.740.8830PG4

Interfaces

1 interface between chains.

  • A–B · 1102 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3BNI · Crystal structure of TetR-family transcriptional regulator from Streptomyces coelicolor · the same entry in another collection · chain A against A, TM-score 1.00

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