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Atomic resolution structure of resting state of the achromobacter cycloclastes cu nitrite reductase

Analyse Atomic resolution structure of resting state of the achromobacter cycloclastes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BW4
Type
protein
Length
334 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Copper-containing nitrite reductase
EC
1.7.2.1
UniProt
P25006
Ligands
CU, SO4
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACopper-containing nitrite reductase (EC 1.7.2.1)protein33411% helix, 40% strandP25006

Ligands and binding sites

  • CU · Copper (II) ion · metal · 2 copies · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • ACT · Acetate ion · additive · 4 copies · chains A
  • MLI · Malonate ion · additive · chains A

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
12310.710.8728empty

Compared structures

  • 2BW4 · Atomic Resolution Structure of Resting State of the Achromobacter cycloclastes Cu Nitrite… · the same entry in another collection · chain A against A, TM-score 1.00
  • P25006 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (P25006) · a predicted model of the same protein · chain A against A, TM-score 0.99

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