1OFE
Glutamate Synthase from Synechocystis sp in complex with 2-Oxoglutarate and L-DON at 2.45 Angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006537 | biological_process | glutamate biosynthetic process |
A | 0006541 | biological_process | glutamine metabolic process |
A | 0015930 | molecular_function | glutamate synthase activity |
A | 0016040 | molecular_function | glutamate synthase (NADH) activity |
A | 0016041 | molecular_function | glutamate synthase (ferredoxin) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
A | 0019676 | biological_process | ammonia assimilation cycle |
A | 0046872 | molecular_function | metal ion binding |
A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
A | 0097054 | biological_process | L-glutamate biosynthetic process |
B | 0006537 | biological_process | glutamate biosynthetic process |
B | 0006541 | biological_process | glutamine metabolic process |
B | 0015930 | molecular_function | glutamate synthase activity |
B | 0016040 | molecular_function | glutamate synthase (NADH) activity |
B | 0016041 | molecular_function | glutamate synthase (ferredoxin) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
B | 0019676 | biological_process | ammonia assimilation cycle |
B | 0046872 | molecular_function | metal ion binding |
B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
B | 0097054 | biological_process | L-glutamate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S B 2509 |
Chain | Residue |
B | MET1132 |
B | CYS1137 |
B | ILE1138 |
B | ARG1141 |
B | VAL1142 |
B | CYS1143 |
B | CYS1148 |
B | VAL1152 |
B | ALA1153 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FMN A 2508 |
Chain | Residue |
A | GLY874 |
A | MET875 |
A | SER876 |
A | GLU903 |
A | GLN944 |
A | LYS966 |
A | GLN969 |
A | LYS1034 |
A | GLY1063 |
A | GLY1064 |
A | THR1065 |
A | GLY1066 |
A | ASP1105 |
A | GLY1106 |
A | GLY1107 |
A | GLY1128 |
A | SER1129 |
A | ILE1130 |
A | MET1132 |
A | HOH2152 |
A | HOH2206 |
A | AKG2510 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F3S A 2509 |
Chain | Residue |
A | MET1132 |
A | CYS1137 |
A | ILE1138 |
A | ARG1141 |
A | VAL1142 |
A | CYS1143 |
A | CYS1148 |
A | ALA1153 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AKG A 2510 |
Chain | Residue |
A | SER876 |
A | ALA879 |
A | GLN969 |
A | LYS972 |
A | GLY977 |
A | GLN978 |
A | ARG992 |
A | THR1065 |
A | GLY1066 |
A | ALA1067 |
A | HOH2207 |
A | HOH2208 |
A | FMN2508 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ONL A 2511 |
Chain | Residue |
A | CYS1 |
A | ARG206 |
A | PHE207 |
A | GLN219 |
A | HIS226 |
A | ASN227 |
A | GLY228 |
A | GLU229 |
A | ASP270 |
A | SER271 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE FMN B 2508 |
Chain | Residue |
B | GLY874 |
B | MET875 |
B | SER876 |
B | GLY902 |
B | GLU903 |
B | GLN944 |
B | LYS966 |
B | GLN969 |
B | LYS1034 |
B | GLY1063 |
B | GLY1064 |
B | THR1065 |
B | GLY1066 |
B | ASP1105 |
B | GLY1107 |
B | PHE1127 |
B | GLY1128 |
B | SER1129 |
B | ILE1130 |
B | MET1132 |
B | AKG2510 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AKG B 2510 |
Chain | Residue |
B | SER876 |
B | ALA879 |
B | GLN969 |
B | LYS972 |
B | GLY977 |
B | GLN978 |
B | ARG992 |
B | THR1065 |
B | GLY1066 |
B | FMN2508 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ONL B 2511 |
Chain | Residue |
B | GLY228 |
B | GLU229 |
B | ASP270 |
B | SER271 |
B | CYS1 |
B | ARG206 |
B | PHE207 |
B | GLN219 |
B | HIS226 |
B | ASN227 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: For GATase activity => ECO:0000250 |
Chain | Residue | Details |
A | CYS1 | |
B | CYS1 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | CYS1137 | |
A | CYS1143 | |
A | CYS1148 | |
B | CYS1137 | |
B | CYS1143 | |
B | CYS1148 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1jxa |
Chain | Residue | Details |
A | TYR659 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1jxa |
Chain | Residue | Details |
B | TYR659 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1jxa |
Chain | Residue | Details |
A | LYS972 | |
A | GLU903 | |
A | CYS1 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1jxa |
Chain | Residue | Details |
B | LYS972 | |
B | GLU903 | |
B | CYS1 |
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 111 |
Chain | Residue | Details |
A | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG31 | activator, electrostatic stabiliser, hydrogen bond acceptor |
A | PHE207 | electrostatic stabiliser, hydrogen bond donor |
A | ASN227 | electrostatic stabiliser, hydrogen bond donor |
A | GLY228 | electrostatic stabiliser, hydrogen bond donor |
A | GLU903 | electrostatic stabiliser, hydrogen bond acceptor |
A | GLN969 | electrostatic stabiliser, hydrogen bond acceptor |
A | LYS972 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLN978 | activator, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 111 |
Chain | Residue | Details |
B | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG31 | activator, electrostatic stabiliser, hydrogen bond acceptor |
B | PHE207 | electrostatic stabiliser, hydrogen bond donor |
B | ASN227 | electrostatic stabiliser, hydrogen bond donor |
B | GLY228 | electrostatic stabiliser, hydrogen bond donor |
B | GLU903 | electrostatic stabiliser, hydrogen bond acceptor |
B | GLN969 | electrostatic stabiliser, hydrogen bond acceptor |
B | LYS972 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLN978 | activator, hydrogen bond donor |