1CF2
THREE-DIMENSIONAL STRUCTURE OF D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON METHANOTHERMUS FERVIDUS
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0005737 | cellular_component | cytoplasm |
O | 0006096 | biological_process | glycolytic process |
O | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
O | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
O | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity |
O | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0005737 | cellular_component | cytoplasm |
P | 0006096 | biological_process | glycolytic process |
P | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
P | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
P | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity |
P | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
P | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0006096 | biological_process | glycolytic process |
Q | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
Q | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
Q | 0016491 | molecular_function | oxidoreductase activity |
Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Q | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity |
Q | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
Q | 0050661 | molecular_function | NADP binding |
Q | 0051287 | molecular_function | NAD binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0005737 | cellular_component | cytoplasm |
R | 0006096 | biological_process | glycolytic process |
R | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
R | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
R | 0016491 | molecular_function | oxidoreductase activity |
R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
R | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity |
R | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
R | 0050661 | molecular_function | NADP binding |
R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 P 1001 |
Chain | Residue |
P | SER139 |
P | CYS140 |
P | ASN141 |
P | ARG167 |
P | HIS193 |
P | HIS194 |
P | HOH1216 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 R 1002 |
Chain | Residue |
R | ASN141 |
R | ARG167 |
R | HIS193 |
R | HIS194 |
R | SER139 |
R | CYS140 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 O 1003 |
Chain | Residue |
O | SER139 |
O | CYS140 |
O | ASN141 |
O | ARG167 |
O | HIS193 |
O | HIS194 |
O | HOH1045 |
O | HOH1126 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 Q 1004 |
Chain | Residue |
Q | SER139 |
Q | CYS140 |
Q | ASN141 |
Q | ARG167 |
Q | HIS193 |
Q | HIS194 |
Q | HOH1212 |
site_id | AC5 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NAP P 340 |
Chain | Residue |
P | ASN7 |
P | GLY8 |
P | TYR9 |
P | GLY10 |
P | THR11 |
P | VAL12 |
P | LYS33 |
P | THR34 |
P | ARG35 |
P | ALA53 |
P | CYS85 |
P | THR86 |
P | PRO87 |
P | GLU88 |
P | ILE90 |
P | GLN108 |
P | GLY110 |
P | ARG168 |
P | ASP171 |
P | GLN300 |
P | HOH1048 |
P | HOH1053 |
P | HOH1061 |
P | HOH1069 |
P | HOH1078 |
P | HOH1088 |
P | HOH1096 |
P | HOH1097 |
P | HOH1104 |
P | HOH1107 |
P | HOH1109 |
P | HOH1111 |
P | HOH1165 |
P | HOH1229 |
P | HOH1232 |
site_id | AC6 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAP R 340 |
Chain | Residue |
R | ASN7 |
R | GLY8 |
R | TYR9 |
R | GLY10 |
R | THR11 |
R | VAL12 |
R | LYS33 |
R | THR34 |
R | ARG35 |
R | CYS85 |
R | THR86 |
R | PRO87 |
R | GLU88 |
R | GLN108 |
R | GLY110 |
R | ASP171 |
R | GLN300 |
R | HOH1006 |
R | HOH1008 |
R | HOH1012 |
R | HOH1015 |
R | HOH1016 |
R | HOH1018 |
R | HOH1104 |
R | HOH1112 |
R | HOH1176 |
site_id | AC7 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAP O 340 |
Chain | Residue |
O | THR86 |
O | PRO87 |
O | GLU88 |
O | GLN108 |
O | GLY110 |
O | ASP171 |
O | GLN300 |
O | ILE304 |
O | HOH1029 |
O | HOH1039 |
O | HOH1048 |
O | HOH1061 |
O | HOH1066 |
O | HOH1071 |
O | HOH1078 |
O | HOH1085 |
O | HOH1103 |
O | HOH1106 |
O | HOH1161 |
O | HOH1172 |
O | HOH1192 |
O | ASN7 |
O | GLY8 |
O | TYR9 |
O | GLY10 |
O | THR11 |
O | VAL12 |
O | LYS33 |
O | THR34 |
O | ARG35 |
O | CYS85 |
site_id | AC8 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAP Q 340 |
Chain | Residue |
Q | ASN7 |
Q | GLY8 |
Q | TYR9 |
Q | GLY10 |
Q | THR11 |
Q | VAL12 |
Q | LYS33 |
Q | THR34 |
Q | ARG35 |
Q | CYS85 |
Q | THR86 |
Q | PRO87 |
Q | GLU88 |
Q | ILE90 |
Q | GLN108 |
Q | GLY110 |
Q | ARG168 |
Q | ASP171 |
Q | GLN300 |
Q | ILE304 |
Q | HOH1051 |
Q | HOH1064 |
Q | HOH1079 |
Q | HOH1087 |
Q | HOH1088 |
Q | HOH1099 |
Q | HOH1104 |
Q | HOH1109 |
Q | HOH1112 |
Q | HOH1124 |
Q | HOH1202 |
Q | HOH1213 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. VSCNTTgL |
Chain | Residue | Details |
P | VAL138-LEU145 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
P | CYS140 | |
R | CYS140 | |
O | CYS140 | |
Q | CYS140 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10715215 |
Chain | Residue | Details |
R | THR11 | |
R | THR34 | |
R | GLY110 | |
R | ASP171 | |
O | THR11 | |
O | THR34 | |
O | GLY110 | |
O | ASP171 | |
Q | THR11 | |
Q | THR34 | |
Q | GLY110 | |
Q | ASP171 | |
P | THR11 | |
P | THR34 | |
P | GLY110 | |
P | ASP171 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
R | HIS194 | |
R | GLN300 | |
O | SER139 | |
O | HIS194 | |
O | GLN300 | |
Q | SER139 | |
Q | HIS194 | |
Q | GLN300 | |
P | SER139 | |
P | HIS194 | |
P | GLN300 | |
R | SER139 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 619 |
Chain | Residue | Details |
P | CYS140 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
P | HIS219 | electrostatic stabiliser, modifies pKa, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 619 |
Chain | Residue | Details |
R | CYS140 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
R | HIS219 | electrostatic stabiliser, modifies pKa, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 619 |
Chain | Residue | Details |
O | CYS140 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
O | HIS219 | electrostatic stabiliser, modifies pKa, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 619 |
Chain | Residue | Details |
Q | CYS140 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
Q | HIS219 | electrostatic stabiliser, modifies pKa, proton acceptor, proton donor |