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Foxe P43212 crystal structure of rhodopseudomonas ferrooxidans SW2 putative iron oxidase

Analyse Foxe P43212 crystal structure of rhodopseudomonas ferrooxidans SW2 putative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MVO
Type
protein
Length
769 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Foxe
UniProt
A3DTD8
Ligands
HEC, CU, PO4
Pockets
13 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFoxeprotein25138% helix, 4% strandA3DTD8
B, CFoxeprotein25940% helix, 3% strandA3DTD8

Ligands and binding sites

  • HEC · Heme C · ligand · 6 copies · chains A, B, C
  • CU · Copper (II) ion · metal · 2 copies · chains B, C
  • PO4 · Phosphate ion · ion · 6 copies · chains A, B, C

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

Pockets

13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15280.790.8557HEC
24800.750.8357HEC
34340.750.8451HEC
44000.750.8443HEC, PO4
53140.730.8533HEC, PO4

Interfaces

3 interfaces between chains.

  • B–C · 1076 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 1069 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 1064 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 cofactor, 3 disulfide (heme c attachment, disulfide).

Compared structures

  • 5MVO · FoxE P43212 crystal structure of Rhodopseudomonas ferrooxidans SW2 putative iron oxidase · the same entry in another collection · chain A against A, TM-score 1.00

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