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Crystal structure of proteus mirabilis transcriptional regulator protein crl at 1.95A resolution

Analyse Crystal structure of proteus mirabilis transcriptional regulator protein crl at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4Q11
Type
protein
Length
252 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sigma factor-binding protein crl
UniProt
B4EUU9
Pockets
1 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASigma factor-binding protein crlprotein12637% helix, 34% strandB4EUU9
BSigma factor-binding protein crlprotein12636% helix, 33% strandB4EUU9

Ligands and binding sites

  • NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11150.520.8120empty

Interfaces

1 interface between chains.

  • A–B · 724 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 4Q11 · Crystal structure of Proteus mirabilis transcriptional regulator protein Crl at 1.95A… · the same entry in another collection · chain A against A, TM-score 1.00

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