1VNI
CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS: RECOMBINANT HOLO-CHLOROPEROXIDASE
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE VO4 A 610 |
Chain | Residue |
A | LYS353 |
A | ARG360 |
A | PHE397 |
A | SER402 |
A | GLY403 |
A | HIS404 |
A | ARG490 |
A | HIS496 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:8552646 |
Chain | Residue | Details |
A | HIS404 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8552646, ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ, ECO:0007744|PDB:1VNC |
Chain | Residue | Details |
A | LYS353 | |
A | ARG360 | |
A | SER402 | |
A | GLY403 | |
A | HIS404 | |
A | ARG490 | |
A | HIS496 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1vnc |
Chain | Residue | Details |
A | LYS353 | |
A | HIS404 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 14 |
Chain | Residue | Details |
A | LYS353 | electrostatic stabiliser, hydrogen bond donor |
A | ARG360 | electrostatic stabiliser, hydrogen bond donor |
A | SER402 | electrostatic stabiliser, hydrogen bond donor |
A | GLY403 | electrostatic stabiliser, hydrogen bond donor |
A | HIS404 | activator, hydrogen bond acceptor |
A | ARG490 | electrostatic stabiliser, hydrogen bond donor |
A | HIS496 | covalently attached, metal ligand |