2VDC
THE 9.5 A RESOLUTION STRUCTURE OF GLUTAMATE SYNTHASE FROM CRYO-ELECTRON MICROSCOPY AND ITS OLIGOMERIZATION BEHAVIOR IN SOLUTION: FUNCTIONAL IMPLICATIONS.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
A | 0006537 | biological_process | glutamate biosynthetic process |
A | 0006541 | biological_process | glutamine metabolic process |
A | 0015930 | molecular_function | glutamate synthase 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 | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
B | 0006537 | biological_process | glutamate biosynthetic process |
B | 0006541 | biological_process | glutamine metabolic process |
B | 0015930 | molecular_function | glutamate synthase 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 |
C | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
C | 0006537 | biological_process | glutamate biosynthetic process |
C | 0006541 | biological_process | glutamine metabolic process |
C | 0015930 | molecular_function | glutamate synthase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
C | 0019676 | biological_process | ammonia assimilation cycle |
C | 0046872 | molecular_function | metal ion binding |
C | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
C | 0097054 | biological_process | L-glutamate biosynthetic process |
D | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
D | 0006537 | biological_process | glutamate biosynthetic process |
D | 0006541 | biological_process | glutamine metabolic process |
D | 0015930 | molecular_function | glutamate synthase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
D | 0019676 | biological_process | ammonia assimilation cycle |
D | 0046872 | molecular_function | metal ion binding |
D | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
D | 0097054 | biological_process | L-glutamate biosynthetic process |
E | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
E | 0006537 | biological_process | glutamate biosynthetic process |
E | 0006541 | biological_process | glutamine metabolic process |
E | 0015930 | molecular_function | glutamate synthase activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
E | 0019676 | biological_process | ammonia assimilation cycle |
E | 0046872 | molecular_function | metal ion binding |
E | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
E | 0097054 | biological_process | L-glutamate biosynthetic process |
F | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
F | 0006537 | biological_process | glutamate biosynthetic process |
F | 0006541 | biological_process | glutamine metabolic process |
F | 0015930 | molecular_function | glutamate synthase activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
F | 0019676 | biological_process | ammonia assimilation cycle |
F | 0046872 | molecular_function | metal ion binding |
F | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
F | 0097054 | biological_process | L-glutamate biosynthetic process |
G | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
G | 0006537 | biological_process | glutamate biosynthetic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0046872 | molecular_function | metal ion binding |
G | 0051536 | molecular_function | iron-sulfur cluster binding |
G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
G | 0097054 | biological_process | L-glutamate biosynthetic process |
H | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
H | 0006537 | biological_process | glutamate biosynthetic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0046872 | molecular_function | metal ion binding |
H | 0051536 | molecular_function | iron-sulfur cluster binding |
H | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
H | 0097054 | biological_process | L-glutamate biosynthetic process |
I | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
I | 0006537 | biological_process | glutamate biosynthetic process |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0046872 | molecular_function | metal ion binding |
I | 0051536 | molecular_function | iron-sulfur cluster binding |
I | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
I | 0097054 | biological_process | L-glutamate biosynthetic process |
J | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
J | 0006537 | biological_process | glutamate biosynthetic process |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0046872 | molecular_function | metal ion binding |
J | 0051536 | molecular_function | iron-sulfur cluster binding |
J | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
J | 0097054 | biological_process | L-glutamate biosynthetic process |
K | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
K | 0006537 | biological_process | glutamate biosynthetic process |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0046872 | molecular_function | metal ion binding |
K | 0051536 | molecular_function | iron-sulfur cluster binding |
K | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
K | 0097054 | biological_process | L-glutamate biosynthetic process |
L | 0004355 | molecular_function | glutamate synthase (NADPH) activity |
L | 0006537 | biological_process | glutamate biosynthetic process |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0046872 | molecular_function | metal ion binding |
L | 0051536 | molecular_function | iron-sulfur cluster binding |
L | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
L | 0097054 | biological_process | L-glutamate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OMT A 2473 |
Chain | Residue |
A | CYS1 |
A | ARG210 |
A | TYR211 |
A | GLN223 |
A | ASN231 |
A | GLY232 |
A | GLU233 |
A | ASP273 |
A | SER274 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE FMN A 2474 |
Chain | Residue |
A | PRO856 |
A | GLY857 |
A | MET858 |
A | SER859 |
A | GLY885 |
A | GLU886 |
A | GLN909 |
A | LYS931 |
A | LYS999 |
A | GLY1028 |
A | GLY1029 |
A | THR1030 |
A | GLY1031 |
A | ASP1070 |
A | GLY1071 |
A | GLY1072 |
A | GLY1093 |
A | THR1094 |
A | AKG2475 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AKG A 2475 |
Chain | Residue |
A | SER859 |
A | GLN934 |
A | LYS937 |
A | GLY942 |
A | GLN943 |
A | ARG957 |
A | THR1030 |
A | GLY1031 |
A | FMN2474 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S A 2476 |
Chain | Residue |
A | CYS1102 |
A | ILE1103 |
A | MET1104 |
A | VAL1105 |
A | ARG1106 |
A | GLN1107 |
A | CYS1108 |
A | CYS1113 |
A | VAL1117 |
A | CYS1118 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE OMT B 2473 |
Chain | Residue |
B | CYS1 |
B | GLN209 |
B | ARG210 |
B | TYR211 |
B | GLN223 |
B | ASN231 |
B | GLY232 |
B | GLU233 |
B | ASP273 |
B | SER274 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE FMN B 2474 |
Chain | Residue |
B | PRO856 |
B | GLY857 |
B | MET858 |
B | SER859 |
B | GLU886 |
B | GLN909 |
B | LYS931 |
B | LYS999 |
B | GLY1028 |
B | GLY1029 |
B | THR1030 |
B | GLY1031 |
B | ASP1070 |
B | GLY1071 |
B | GLY1072 |
B | GLY1093 |
B | THR1094 |
B | AKG2475 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AKG B 2475 |
Chain | Residue |
B | SER859 |
B | GLN934 |
B | LYS937 |
B | GLY942 |
B | GLN943 |
B | ARG957 |
B | THR1030 |
B | GLY1031 |
B | ALA1032 |
B | FMN2474 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S B 2476 |
Chain | Residue |
B | CYS1102 |
B | ILE1103 |
B | MET1104 |
B | VAL1105 |
B | ARG1106 |
B | GLN1107 |
B | CYS1108 |
B | CYS1113 |
B | VAL1117 |
B | CYS1118 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OMT C 2473 |
Chain | Residue |
C | ASN231 |
C | GLY232 |
C | GLU233 |
C | ASP273 |
C | SER274 |
C | CYS1 |
C | ARG210 |
C | TYR211 |
C | GLN223 |
site_id | BC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE FMN C 2474 |
Chain | Residue |
C | PRO856 |
C | GLY857 |
C | MET858 |
C | SER859 |
C | GLY885 |
C | GLU886 |
C | GLN909 |
C | LYS931 |
C | LYS999 |
C | GLY1028 |
C | GLY1029 |
C | THR1030 |
C | GLY1031 |
C | ASP1070 |
C | GLY1071 |
C | GLY1072 |
C | GLY1093 |
C | THR1094 |
C | AKG2475 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AKG C 2475 |
Chain | Residue |
C | SER859 |
C | GLN934 |
C | LYS937 |
C | GLY942 |
C | GLN943 |
C | ARG957 |
C | THR1030 |
C | GLY1031 |
C | FMN2474 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S C 2476 |
Chain | Residue |
C | CYS1102 |
C | ILE1103 |
C | MET1104 |
C | VAL1105 |
C | ARG1106 |
C | GLN1107 |
C | CYS1108 |
C | CYS1113 |
C | VAL1117 |
C | CYS1118 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE OMT D 2473 |
Chain | Residue |
D | CYS1 |
D | GLN209 |
D | ARG210 |
D | TYR211 |
D | GLN223 |
D | ASN231 |
D | GLY232 |
D | GLU233 |
D | ASP273 |
D | SER274 |
site_id | BC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE FMN D 2474 |
Chain | Residue |
D | PRO856 |
D | GLY857 |
D | MET858 |
D | SER859 |
D | GLU886 |
D | GLN909 |
D | LYS931 |
D | LYS999 |
D | GLY1028 |
D | GLY1029 |
D | THR1030 |
D | GLY1031 |
D | ASP1070 |
D | GLY1071 |
D | GLY1072 |
D | GLY1093 |
D | THR1094 |
D | AKG2475 |
site_id | BC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AKG D 2475 |
Chain | Residue |
D | SER859 |
D | GLN934 |
D | LYS937 |
D | GLY942 |
D | GLN943 |
D | ARG957 |
D | THR1030 |
D | GLY1031 |
D | ALA1032 |
D | FMN2474 |
site_id | BC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S D 2476 |
Chain | Residue |
D | CYS1102 |
D | ILE1103 |
D | MET1104 |
D | VAL1105 |
D | ARG1106 |
D | GLN1107 |
D | CYS1108 |
D | CYS1113 |
D | VAL1117 |
D | CYS1118 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE OMT E 2473 |
Chain | Residue |
E | CYS1 |
E | ARG210 |
E | TYR211 |
E | GLN223 |
E | ASN231 |
E | GLY232 |
E | GLU233 |
E | ASP273 |
E | SER274 |
site_id | BC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE FMN E 2474 |
Chain | Residue |
E | PRO856 |
E | GLY857 |
E | MET858 |
E | SER859 |
E | GLY885 |
E | GLU886 |
E | GLN909 |
E | LYS931 |
E | LYS999 |
E | GLY1028 |
E | GLY1029 |
E | THR1030 |
E | GLY1031 |
E | ASP1070 |
E | GLY1071 |
E | GLY1072 |
E | GLY1093 |
E | THR1094 |
E | AKG2475 |
site_id | CC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AKG E 2475 |
Chain | Residue |
E | SER859 |
E | GLN934 |
E | LYS937 |
E | GLY942 |
E | GLN943 |
E | ARG957 |
E | THR1030 |
E | GLY1031 |
E | FMN2474 |
site_id | CC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S E 2476 |
Chain | Residue |
E | CYS1102 |
E | ILE1103 |
E | MET1104 |
E | VAL1105 |
E | ARG1106 |
E | GLN1107 |
E | CYS1108 |
E | CYS1113 |
E | VAL1117 |
E | CYS1118 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE OMT F 2473 |
Chain | Residue |
F | CYS1 |
F | GLN209 |
F | ARG210 |
F | TYR211 |
F | GLN223 |
F | ASN231 |
F | GLY232 |
F | GLU233 |
F | ASP273 |
F | SER274 |
site_id | CC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE FMN F 2474 |
Chain | Residue |
F | PRO856 |
F | GLY857 |
F | MET858 |
F | SER859 |
F | GLU886 |
F | GLN909 |
F | LYS931 |
F | LYS999 |
F | GLY1028 |
F | GLY1029 |
F | THR1030 |
F | GLY1031 |
F | ASP1070 |
F | GLY1071 |
F | GLY1072 |
F | GLY1093 |
F | THR1094 |
F | AKG2475 |
site_id | CC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AKG F 2475 |
Chain | Residue |
F | SER859 |
F | GLN934 |
F | LYS937 |
F | GLY942 |
F | GLN943 |
F | ARG957 |
F | THR1030 |
F | GLY1031 |
F | ALA1032 |
F | FMN2474 |
site_id | CC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S F 2476 |
Chain | Residue |
F | CYS1102 |
F | ILE1103 |
F | MET1104 |
F | VAL1105 |
F | ARG1106 |
F | GLN1107 |
F | CYS1108 |
F | CYS1113 |
F | VAL1117 |
F | CYS1118 |
site_id | CC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 G 482 |
Chain | Residue |
G | CYS59 |
G | ILE65 |
G | ASN88 |
G | CYS98 |
G | GLN100 |
G | LEU103 |
G | CYS104 |
G | GLU124 |
site_id | CC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 G 483 |
Chain | Residue |
G | CYS47 |
G | SER48 |
G | CYS50 |
G | CYS55 |
G | CYS108 |
G | VAL109 |
G | ILE110 |
G | VAL118 |
G | ILE120 |
site_id | CC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD G 484 |
Chain | Residue |
G | ILE97 |
G | ILE153 |
G | GLY154 |
G | GLY156 |
G | PRO157 |
G | ALA158 |
G | ASP177 |
G | ARG178 |
G | TYR179 |
G | GLY184 |
G | LEU185 |
G | LYS194 |
G | GLU219 |
G | VAL220 |
G | ALA239 |
G | THR240 |
G | GLY241 |
G | LEU265 |
G | ASP299 |
G | THR300 |
G | ASP303 |
G | ASN408 |
G | GLY441 |
G | ASP442 |
G | SER448 |
G | LEU449 |
G | VAL450 |
G | ALA453 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 H 482 |
Chain | Residue |
H | CYS59 |
H | ILE65 |
H | ASN88 |
H | CYS98 |
H | GLN100 |
H | LEU103 |
H | CYS104 |
H | GLU124 |
site_id | DC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 H 483 |
Chain | Residue |
H | CYS47 |
H | SER48 |
H | CYS50 |
H | CYS55 |
H | CYS108 |
H | VAL109 |
H | ILE110 |
H | VAL118 |
H | ILE120 |
site_id | DC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD H 484 |
Chain | Residue |
H | ILE97 |
H | ILE153 |
H | GLY154 |
H | GLY156 |
H | PRO157 |
H | ALA158 |
H | ASP177 |
H | ARG178 |
H | TYR179 |
H | GLY184 |
H | LEU185 |
H | LYS194 |
H | GLU219 |
H | VAL220 |
H | ALA239 |
H | THR240 |
H | GLY241 |
H | LEU265 |
H | ASP299 |
H | THR300 |
H | ASP303 |
H | ASN408 |
H | GLY441 |
H | ASP442 |
H | SER448 |
H | LEU449 |
H | VAL450 |
H | ALA453 |
site_id | DC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 I 482 |
Chain | Residue |
I | CYS59 |
I | ILE65 |
I | ASN88 |
I | CYS98 |
I | GLN100 |
I | LEU103 |
I | CYS104 |
I | GLU124 |
site_id | DC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 I 483 |
Chain | Residue |
I | CYS47 |
I | SER48 |
I | CYS50 |
I | CYS55 |
I | CYS108 |
I | VAL109 |
I | ILE110 |
I | VAL118 |
I | ILE120 |
site_id | DC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD I 484 |
Chain | Residue |
I | ILE97 |
I | ILE153 |
I | GLY154 |
I | GLY156 |
I | PRO157 |
I | ALA158 |
I | ASP177 |
I | ARG178 |
I | TYR179 |
I | GLY184 |
I | LEU185 |
I | LYS194 |
I | GLU219 |
I | VAL220 |
I | ALA239 |
I | THR240 |
I | GLY241 |
I | LEU265 |
I | ASP299 |
I | THR300 |
I | ASP303 |
I | ASN408 |
I | GLY441 |
I | ASP442 |
I | SER448 |
I | LEU449 |
I | VAL450 |
I | ALA453 |
site_id | DC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 J 482 |
Chain | Residue |
J | CYS59 |
J | ILE65 |
J | ASN88 |
J | CYS98 |
J | GLN100 |
J | LEU103 |
J | CYS104 |
J | GLU124 |
site_id | DC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 J 483 |
Chain | Residue |
J | CYS47 |
J | SER48 |
J | CYS50 |
J | CYS55 |
J | CYS108 |
J | VAL109 |
J | ILE110 |
J | VAL118 |
J | ILE120 |
site_id | DC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD J 484 |
Chain | Residue |
J | ILE97 |
J | ILE153 |
J | GLY154 |
J | GLY156 |
J | PRO157 |
J | ALA158 |
J | ASP177 |
J | ARG178 |
J | TYR179 |
J | GLY184 |
J | LEU185 |
J | LYS194 |
J | GLU219 |
J | VAL220 |
J | ALA239 |
J | THR240 |
J | GLY241 |
J | LEU265 |
J | ASP299 |
J | THR300 |
J | ASP303 |
J | ASN408 |
J | GLY441 |
J | ASP442 |
J | SER448 |
J | LEU449 |
J | VAL450 |
J | ALA453 |
site_id | EC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 K 482 |
Chain | Residue |
K | CYS59 |
K | ILE65 |
K | ASN88 |
K | CYS98 |
K | GLN100 |
K | LEU103 |
K | CYS104 |
K | GLU124 |
site_id | EC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 K 483 |
Chain | Residue |
K | CYS47 |
K | SER48 |
K | CYS50 |
K | CYS55 |
K | CYS108 |
K | VAL109 |
K | ILE110 |
K | VAL118 |
K | ILE120 |
site_id | EC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD K 484 |
Chain | Residue |
K | ILE97 |
K | ILE153 |
K | GLY154 |
K | GLY156 |
K | PRO157 |
K | ALA158 |
K | ASP177 |
K | ARG178 |
K | TYR179 |
K | GLY184 |
K | LEU185 |
K | LYS194 |
K | GLU219 |
K | VAL220 |
K | ALA239 |
K | THR240 |
K | GLY241 |
K | LEU265 |
K | ASP299 |
K | THR300 |
K | ASP303 |
K | ASN408 |
K | GLY441 |
K | ASP442 |
K | SER448 |
K | LEU449 |
K | VAL450 |
K | ALA453 |
site_id | EC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 L 482 |
Chain | Residue |
L | CYS59 |
L | ILE65 |
L | ASN88 |
L | CYS98 |
L | GLN100 |
L | LEU103 |
L | CYS104 |
L | GLU124 |
site_id | EC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 L 483 |
Chain | Residue |
L | CYS47 |
L | SER48 |
L | CYS50 |
L | CYS55 |
L | CYS108 |
L | VAL109 |
L | ILE110 |
L | VAL118 |
L | ILE120 |
site_id | EC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD L 484 |
Chain | Residue |
L | ILE97 |
L | ILE153 |
L | GLY154 |
L | GLY156 |
L | PRO157 |
L | ALA158 |
L | ASP177 |
L | ARG178 |
L | TYR179 |
L | GLY184 |
L | LEU185 |
L | LYS194 |
L | GLU219 |
L | VAL220 |
L | ALA239 |
L | THR240 |
L | GLY241 |
L | LEU265 |
L | ASP299 |
L | THR300 |
L | ASP303 |
L | ASN408 |
L | GLY441 |
L | ASP442 |
L | SER448 |
L | LEU449 |
L | VAL450 |
L | ALA453 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
G | CYS94 | |
I | CYS98 | |
I | CYS104 | |
I | CYS108 | |
J | CYS94 | |
J | CYS98 | |
J | CYS104 | |
J | CYS108 | |
K | CYS94 | |
K | CYS98 | |
K | CYS104 | |
G | CYS98 | |
K | CYS108 | |
L | CYS94 | |
L | CYS98 | |
L | CYS104 | |
L | CYS108 | |
G | CYS104 | |
G | CYS108 | |
H | CYS94 | |
H | CYS98 | |
H | CYS104 | |
H | CYS108 | |
I | CYS94 |
site_id | SWS_FT_FI2 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | LEU1049 | |
B | CYS1113 | |
C | LEU1049 | |
C | SER1050 | |
C | CYS1102 | |
C | CYS1108 | |
C | CYS1113 | |
D | LEU1049 | |
D | SER1050 | |
D | CYS1102 | |
D | CYS1108 | |
A | SER1050 | |
D | CYS1113 | |
E | LEU1049 | |
E | SER1050 | |
E | CYS1102 | |
E | CYS1108 | |
E | CYS1113 | |
F | LEU1049 | |
F | SER1050 | |
F | CYS1102 | |
F | CYS1108 | |
A | CYS1102 | |
F | CYS1113 | |
A | CYS1108 | |
A | CYS1113 | |
B | LEU1049 | |
B | SER1050 | |
B | CYS1102 | |
B | CYS1108 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ofd |
Chain | Residue | Details |
A | LYS937 | |
A | GLU886 | |
A | CYS1 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ofd |
Chain | Residue | Details |
B | LYS937 | |
B | GLU886 | |
B | CYS1 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ofd |
Chain | Residue | Details |
C | LYS937 | |
C | GLU886 | |
C | CYS1 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ofd |
Chain | Residue | Details |
D | LYS937 | |
D | GLU886 | |
D | CYS1 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ofd |
Chain | Residue | Details |
E | LYS937 | |
E | GLU886 | |
E | CYS1 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ofd |
Chain | Residue | Details |
F | LYS937 | |
F | GLU886 | |
F | CYS1 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 304 |
Chain | Residue | Details |
A | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ASN231 | electrostatic stabiliser, hydrogen bond donor |
A | GLY232 | electrostatic stabiliser, hydrogen bond donor |
A | MET479 | single electron acceptor, single electron donor, single electron relay |
A | GLU886 | proton acceptor, proton donor, proton relay |
A | LYS937 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 304 |
Chain | Residue | Details |
B | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ASN231 | electrostatic stabiliser, hydrogen bond donor |
B | GLY232 | electrostatic stabiliser, hydrogen bond donor |
B | MET479 | single electron acceptor, single electron donor, single electron relay |
B | GLU886 | proton acceptor, proton donor, proton relay |
B | LYS937 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 304 |
Chain | Residue | Details |
C | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
C | ASN231 | electrostatic stabiliser, hydrogen bond donor |
C | GLY232 | electrostatic stabiliser, hydrogen bond donor |
C | MET479 | single electron acceptor, single electron donor, single electron relay |
C | GLU886 | proton acceptor, proton donor, proton relay |
C | LYS937 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 304 |
Chain | Residue | Details |
D | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
D | ASN231 | electrostatic stabiliser, hydrogen bond donor |
D | GLY232 | electrostatic stabiliser, hydrogen bond donor |
D | MET479 | single electron acceptor, single electron donor, single electron relay |
D | GLU886 | proton acceptor, proton donor, proton relay |
D | LYS937 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 304 |
Chain | Residue | Details |
E | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
E | ASN231 | electrostatic stabiliser, hydrogen bond donor |
E | GLY232 | electrostatic stabiliser, hydrogen bond donor |
E | MET479 | single electron acceptor, single electron donor, single electron relay |
E | GLU886 | proton acceptor, proton donor, proton relay |
E | LYS937 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 304 |
Chain | Residue | Details |
F | CYS1 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
F | ASN231 | electrostatic stabiliser, hydrogen bond donor |
F | GLY232 | electrostatic stabiliser, hydrogen bond donor |
F | MET479 | single electron acceptor, single electron donor, single electron relay |
F | GLU886 | proton acceptor, proton donor, proton relay |
F | LYS937 | electrostatic stabiliser |