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Structure of HI0074 from heamophilus influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase

Analyse Structure of HI0074 from heamophilus influenzae reveals the fold of a substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1JOG
Type
protein
Length
541 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical protein HI0074
UniProt
P43934
Pockets
5 · best druggability 0.45

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CHypothetical protein HI0074protein13578% helix, 0% strandP43934
DHypothetical protein HI0074protein13677% helix, 0% strandP43934

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11210.450.7825empty
2830.450.8121empty
31980.450.7322empty
4750.420.8015empty
51010.350.7412empty

Interfaces

6 interfaces between chains.

  • A–B · 1117 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 1075 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 192 Ų buried · 2 hydrogen bonds · protein-protein
  • A–D · 178 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 161 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

  • 1JOG · Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding… · the same entry in another collection · chain A against A, TM-score 1.00
  • P43934 · AlphaFold monomer V2.0 prediction for probable ribonuclease hept (P43934) · a predicted model of the same protein · chain D against A, TM-score 0.97

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