PDB ID:  pdb_00007w2j
  • Cryo-EM Structure of Membrane-bound Fructose Dehydrogenase from Gluconobacter japonicus
  • Experimental method: ELECTRON MICROSCOPY
  • Resolution: unavailable
  • Deposition date: 2021-11-24
Number of assemblies:  1
Assembly ID:  0  (author_defined_assembly)    
Structural data modeled
Oligomeric count 6
label_asym_ids of protein
label_asym_ids of heme
label_asym_ids of the others G (FADStructure of FADFAD ), H (F3SStructure of F3SF3S ), L (FADStructure of FADFAD ), M (F3SStructure of F3SF3S )
Each chain information

Showing all 6 chains (2 with heme). Show only chains with heme

Chain A  
auth_asym_id A
Residue indices (Uniprot) 6-542 (1-544)
Uniprot ID M1VMF7 →UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain B  
auth_asym_id B
Residue indices (Uniprot) 50-172 (1-183)
Missing residues 99LYS-115ASP:131GLY-131GLY:138ASN-140LYS:151GLN-155ASP
Structural gaps Exists
Uniprot ID M1VB40 →UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.24 Å
Chain C heme  
auth_asym_id C
Residue indices (Uniprot) 40-471 (1-486)
Missing residues 318ALA-331LYS
Structural gaps Exists
Uniprot ID M1V1V5 →UniprotKB
label_asym_ids of heme K ,  J ,  I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.15 Å
Chain D  
auth_asym_id D
Residue indices (Uniprot) 6-542 (1-544)
Uniprot ID M1VMF7 →UniprotKB
label_asym_ids of heme None
Available structure PDB
Chain E  
auth_asym_id E
Residue indices (Uniprot) 50-172 (1-183)
Missing residues 99LYS-115ASP:131GLY-131GLY:138ASN-140LYS:151GLN-155ASP
Structural gaps Exists
Uniprot ID M1VB40 →UniprotKB
label_asym_ids of heme None
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.26 Å
Chain F heme  
auth_asym_id F
Residue indices (Uniprot) 40-471 (1-486)
Missing residues 318ALA-331LYS
Structural gaps Exists
Uniprot ID M1V1V5 →UniprotKB
label_asym_ids of heme P ,  O ,  N
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.14 Å