5LBH
Crystal structure of Helicobacter cinaedi CAIP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008199 | molecular_function | ferric iron binding |
A | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
B | 0008199 | molecular_function | ferric iron binding |
B | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
C | 0008199 | molecular_function | ferric iron binding |
C | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
D | 0008199 | molecular_function | ferric iron binding |
D | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
E | 0008199 | molecular_function | ferric iron binding |
E | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
F | 0008199 | molecular_function | ferric iron binding |
F | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
G | 0008199 | molecular_function | ferric iron binding |
G | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
H | 0008199 | molecular_function | ferric iron binding |
H | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
I | 0008199 | molecular_function | ferric iron binding |
I | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
J | 0008199 | molecular_function | ferric iron binding |
J | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
K | 0008199 | molecular_function | ferric iron binding |
K | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
L | 0008199 | molecular_function | ferric iron binding |
L | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue FE A 201 |
Chain | Residue |
A | ASP51 |
A | GLU55 |
A | HOH328 |
J | HIS24 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue FE B 201 |
Chain | Residue |
B | ASP51 |
B | GLU55 |
B | HOH322 |
E | HIS24 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue FE C 201 |
Chain | Residue |
C | GLU55 |
C | HOH323 |
I | HIS24 |
C | ASP51 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue FE D 201 |
Chain | Residue |
D | ASP51 |
D | GLU55 |
G | HIS24 |
G | HOH319 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue FE E 201 |
Chain | Residue |
B | HIS24 |
E | ASP51 |
E | GLU55 |
E | HOH315 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue FE F 201 |
Chain | Residue |
F | ASP51 |
F | GLU55 |
F | HOH316 |
L | HIS24 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue FE G 201 |
Chain | Residue |
D | HIS24 |
D | HOH328 |
G | ASP51 |
G | GLU55 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue FE H 201 |
Chain | Residue |
H | ASP51 |
H | GLU55 |
K | HIS24 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue FE I 201 |
Chain | Residue |
C | HIS24 |
C | HOH320 |
I | ASP51 |
I | GLU55 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue FE J 201 |
Chain | Residue |
A | HIS24 |
A | HOH327 |
J | ASP51 |
J | GLU55 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue FE K 201 |
Chain | Residue |
H | HIS24 |
K | ASP51 |
K | GLU55 |
K | HOH315 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue FE L 201 |
Chain | Residue |
F | HIS24 |
L | ASP51 |
L | GLU55 |
Functional Information from PROSITE/UniProt
site_id | PS00819 |
Number of Residues | 15 |
Details | DPS_2 Dps protein family signature 2. FDdVAERvlqLGemP |
Chain | Residue | Details |
A | PHE50-PRO64 |