2X9I
Structure of the Mutant D105N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0010024 | biological_process | phytochromobilin biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
A | 0050897 | molecular_function | cobalt ion binding |
B | 0010024 | biological_process | phytochromobilin biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
B | 0050897 | molecular_function | cobalt ion binding |
C | 0010024 | biological_process | phytochromobilin biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
C | 0050897 | molecular_function | cobalt ion binding |
D | 0010024 | biological_process | phytochromobilin biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016636 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor |
D | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1235 |
Chain | Residue |
A | ASP48 |
A | ARG220 |
C | ASP48 |
C | ARG220 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1235 |
Chain | Residue |
B | ASP48 |
B | ARG220 |
D | ASP48 |
D | ARG220 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE BLA C 1234 |
Chain | Residue |
B | PHE143 |
C | ILE79 |
C | ASN88 |
C | ILE90 |
C | GLY103 |
C | MET104 |
C | ASN105 |
C | MET107 |
C | ILE115 |
C | GLN121 |
C | ARG142 |
C | PHE143 |
C | PHE144 |
C | TYR158 |
C | MET202 |
C | ASP206 |
C | PRO207 |
C | VAL208 |
C | TYR211 |
B | ARG142 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BLA D 1234 |
Chain | Residue |
D | ILE79 |
D | ASN88 |
D | GLY103 |
D | MET104 |
D | ASN105 |
D | MET107 |
D | LYS113 |
D | ILE115 |
D | GLN121 |
D | TYR141 |
D | ARG142 |
D | PHE143 |
D | PHE144 |
D | TYR158 |
D | MET202 |
D | ASP206 |
D | VAL208 |
D | TYR211 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE BLA B 1234 |
Chain | Residue |
B | ILE79 |
B | ASN88 |
B | ILE90 |
B | GLY103 |
B | MET104 |
B | ASN105 |
B | MET107 |
B | ILE115 |
B | GLN121 |
B | ARG142 |
B | PHE143 |
B | PHE144 |
B | TYR158 |
B | MET202 |
B | ASP206 |
B | PRO207 |
B | VAL208 |
B | TYR211 |
B | HOH2091 |
C | ARG142 |
C | PHE143 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE BLA A 1234 |
Chain | Residue |
A | ILE79 |
A | ASN88 |
A | ILE90 |
A | GLY103 |
A | MET104 |
A | ASN105 |
A | MET107 |
A | LYS113 |
A | ILE115 |
A | GLN121 |
A | TYR141 |
A | ARG142 |
A | PHE143 |
A | PHE144 |
A | TYR158 |
A | MET202 |
A | ASP206 |
A | PRO207 |
A | VAL208 |
A | TYR211 |
A | HOH2098 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 306 |
Chain | Residue | Details |
A | ASN105 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
A | ASP206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 306 |
Chain | Residue | Details |
B | ASN105 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
B | ASP206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 306 |
Chain | Residue | Details |
C | ASN105 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
C | ASP206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 306 |
Chain | Residue | Details |
D | ASN105 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
D | ASP206 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |