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Structure of N-terminal domain of mtra

Analyse Structure of N-terminal domain of mtra in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3NHZ
Type
protein
Length
469 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Two component system transcriptional regulator mtra
UniProt
C6DXJ2
Ligands
MG
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · 3 distinct chains · 44% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATwo component system transcriptional regulator mtraprotein11744% helix, 22% strandC6DXJ2
BTwo component system transcriptional regulator mtraprotein11643% helix, 22% strandC6DXJ2
C, DTwo component system transcriptional regulator mtraprotein11844% helix, 22% strandC6DXJ2

Ligands and binding sites

  • MG · Magnesium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13550.620.7845empty
2750.370.7614empty

Interfaces

2 interfaces between chains.

  • A–C · 518 Ų buried · 11 hydrogen bonds · protein-protein
  • A–D · 406 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3NHZ · Structure of N-terminal Domain of MtrA · the same entry in another collection · chain A against A, TM-score 1.00

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