1OFD
Glutamate Synthase from Synechocystis sp in complex with 2-Oxoglutarate at 2.0 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006537 | biological_process | glutamate biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0015930 | molecular_function | glutamate synthase 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 | 0051536 | molecular_function | iron-sulfur cluster 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 | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0015930 | molecular_function | glutamate synthase 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 | 0051536 | molecular_function | iron-sulfur cluster 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 | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A 3508 |
| Chain | Residue |
| A | GLY874 |
| A | GLY1063 |
| A | GLY1064 |
| A | THR1065 |
| A | GLY1066 |
| A | ASP1105 |
| A | GLY1106 |
| A | GLY1107 |
| A | GLY1128 |
| A | SER1129 |
| A | ILE1130 |
| A | MET875 |
| A | MET1132 |
| A | HOH2703 |
| A | HOH2704 |
| A | HOH2705 |
| A | AKG3510 |
| A | SER876 |
| A | GLY902 |
| A | GLU903 |
| A | GLN944 |
| A | LYS966 |
| A | GLN969 |
| A | LYS1034 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S A 3509 |
| Chain | Residue |
| A | MET1132 |
| A | CYS1137 |
| A | ILE1138 |
| A | MET1139 |
| A | ALA1140 |
| A | ARG1141 |
| A | VAL1142 |
| A | CYS1143 |
| A | CYS1148 |
| A | ALA1153 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKG A 3510 |
| Chain | Residue |
| A | SER876 |
| A | ALA879 |
| A | GLU903 |
| A | GLN969 |
| A | LYS972 |
| A | GLY977 |
| A | GLN978 |
| A | ARG992 |
| A | THR1065 |
| A | GLY1066 |
| A | HOH2463 |
| A | HOH2487 |
| A | FMN3508 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 3508 |
| 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 | GLY1106 |
| B | GLY1107 |
| B | GLY1128 |
| B | SER1129 |
| B | ILE1130 |
| B | HOH2535 |
| B | HOH2716 |
| B | HOH2717 |
| B | AKG3510 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F3S B 3509 |
| Chain | Residue |
| B | MET1132 |
| B | CYS1137 |
| B | ILE1138 |
| B | MET1139 |
| B | ALA1140 |
| B | ARG1141 |
| B | VAL1142 |
| B | CYS1143 |
| B | CYS1148 |
| B | ALA1153 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AKG B 3510 |
| Chain | Residue |
| B | SER876 |
| B | ALA879 |
| B | GLU903 |
| B | GLN969 |
| B | LYS972 |
| B | GLY977 |
| B | GLN978 |
| B | ARG992 |
| B | THR1065 |
| B | GLY1066 |
| B | ALA1067 |
| B | HOH2718 |
| B | HOH2719 |
| B | FMN3508 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 788 |
| Details | Domain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11967268, 12818206 |
| Chain | Residue | Details |
| A | LYS972 | |
| A | GLU903 | |
| A | CYS1 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 11967268, 12818206 |
| 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 |
