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Crystal structure of abfr of staphylococcus epidermidis

Analyse Crystal structure of abfr of staphylococcus epidermidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4HBL
Type
protein
Length
568 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcriptional regulator, marr family
UniProt
Q5HKZ1
Pockets
5 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 72% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATranscriptional regulator, marr familyprotein13875% helix, 6% strandQ5HKZ1
BTranscriptional regulator, marr familyprotein14174% helix, 9% strandQ5HKZ1
CTranscriptional regulator, marr familyprotein14272% helix, 8% strandQ5HKZ1
DTranscriptional regulator, marr familyprotein14767% helix, 7% strandQ5HKZ1

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111440.810.8288empty
21260.650.8721empty
32680.520.7525empty
42220.480.7430empty
51340.420.7519empty

Interfaces

6 interfaces between chains.

  • A–B · 3316 Ų buried · 29 hydrogen bonds · protein-protein
  • C–D · 3175 Ų buried · 21 hydrogen bonds · protein-protein
  • B–D · 494 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 451 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 282 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 4HBL · Crystal structure of AbfR of Staphylococcus epidermidis · the same entry in another collection · chain A against A, TM-score 1.00

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