Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008127 | molecular_function | quercetin 2,3-dioxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0008127 | molecular_function | quercetin 2,3-dioxygenase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0008127 | molecular_function | quercetin 2,3-dioxygenase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051213 | molecular_function | dioxygenase activity |
D | 0008127 | molecular_function | quercetin 2,3-dioxygenase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051213 | molecular_function | dioxygenase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS66 | |
C | HIS68 | |
C | GLU73 | |
C | HIS112 | |
D | HIS66 | |
D | HIS68 | |
D | GLU73 | |
D | HIS112 | |
A | HIS68 | |
A | GLU73 | |
A | HIS112 | |
B | HIS66 | |
B | HIS68 | |
B | GLU73 | |
B | HIS112 | |
C | HIS66 | |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN90 | |
B | ASN248 | |
C | ASN90 | |
C | ASN109 | |
C | ASN142 | |
C | ASN191 | |
C | ASN248 | |
D | ASN90 | |
D | ASN109 | |
D | ASN142 | |
D | ASN191 | |
A | ASN109 | |
D | ASN248 | |
A | ASN142 | |
A | ASN191 | |
A | ASN248 | |
B | ASN90 | |
B | ASN109 | |
B | ASN142 | |
B | ASN191 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1gqg |
Chain | Residue | Details |
A | GLU73 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1gqg |
Chain | Residue | Details |
B | GLU73 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1gqg |
Chain | Residue | Details |
C | GLU73 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1gqg |
Chain | Residue | Details |
D | GLU73 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 743 |
Chain | Residue | Details |
A | HIS66 | metal ligand |
A | HIS68 | metal ligand |
A | GLU73 | electrostatic stabiliser, proton acceptor, proton donor |
A | HIS112 | metal ligand |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 743 |
Chain | Residue | Details |
B | HIS66 | metal ligand |
B | HIS68 | metal ligand |
B | GLU73 | electrostatic stabiliser, proton acceptor, proton donor |
B | HIS112 | metal ligand |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 743 |
Chain | Residue | Details |
C | HIS66 | metal ligand |
C | HIS68 | metal ligand |
C | GLU73 | electrostatic stabiliser, proton acceptor, proton donor |
C | HIS112 | metal ligand |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 743 |
Chain | Residue | Details |
D | HIS66 | metal ligand |
D | HIS68 | metal ligand |
D | GLU73 | electrostatic stabiliser, proton acceptor, proton donor |
D | HIS112 | metal ligand |