6H2R
Sulfolobus solfataricus 2-keto-3-deoxygluconate aldolase T157V/D181Q/A198L variant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008674 | molecular_function | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity |
A | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
A | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
A | 0016829 | molecular_function | lyase activity |
B | 0008674 | molecular_function | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity |
B | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
B | 0016829 | molecular_function | lyase activity |
C | 0008674 | molecular_function | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity |
C | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
C | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
C | 0016829 | molecular_function | lyase activity |
D | 0008674 | molecular_function | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase activity |
D | 0008675 | molecular_function | 2-dehydro-3-deoxy-phosphogluconate aldolase activity |
D | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue IPA A 301 |
Chain | Residue |
A | HIS125 |
A | HOH436 |
A | HOH503 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue IPA A 302 |
Chain | Residue |
A | LEU198 |
A | PRO7 |
A | THR43 |
A | THR44 |
A | TYR130 |
A | TYR132 |
A | VAL157 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | GLY240 |
A | SER241 |
A | LEU242 |
A | SER243 |
A | PRO263 |
A | ILE264 |
B | ARG106 |
B | MET107 |
B | SER108 |
B | HIS111 |
B | HOH414 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | ILE93 |
A | PRO124 |
A | HIS125 |
A | PRO126 |
A | HOH409 |
A | HOH439 |
A | HOH440 |
A | HOH600 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue IPA B 301 |
Chain | Residue |
B | PRO7 |
B | THR43 |
B | THR44 |
B | TYR130 |
B | VAL157 |
B | LEU198 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
A | ARG106 |
A | MET107 |
A | SER108 |
A | HIS111 |
B | GLY240 |
B | SER241 |
B | LEU242 |
B | SER243 |
B | PRO263 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue PGE B 303 |
Chain | Residue |
A | TYR103 |
A | TYR104 |
A | THR134 |
A | ALA135 |
A | THR136 |
A | GLY137 |
A | LYS138 |
A | HOH499 |
B | TYR103 |
B | TYR104 |
B | THR134 |
B | ALA135 |
B | THR136 |
B | GLY137 |
B | LYS138 |
B | HOH468 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue IPA C 301 |
Chain | Residue |
C | CYS120 |
C | HOH475 |
C | HOH535 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue IPA C 302 |
Chain | Residue |
C | PRO7 |
C | THR43 |
C | THR44 |
C | TYR130 |
C | TYR132 |
C | VAL157 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL C 303 |
Chain | Residue |
C | GLY240 |
C | SER241 |
C | LEU242 |
C | SER243 |
C | PRO263 |
D | ARG106 |
D | MET107 |
D | SER108 |
D | HIS111 |
site_id | AD2 |
Number of Residues | 16 |
Details | binding site for residue PGE C 304 |
Chain | Residue |
C | TYR103 |
C | TYR104 |
C | THR134 |
C | ALA135 |
C | THR136 |
C | GLY137 |
C | LYS138 |
C | HOH460 |
D | TYR103 |
D | TYR104 |
D | THR134 |
D | ALA135 |
D | THR136 |
D | GLY137 |
D | LYS138 |
D | HOH475 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue IPA D 301 |
Chain | Residue |
D | VAL157 |
D | LEU198 |
D | PRO7 |
D | THR43 |
D | THR44 |
D | TYR130 |
D | TYR132 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue GOL D 302 |
Chain | Residue |
C | ARG106 |
C | MET107 |
C | SER108 |
C | HIS111 |
D | GLY240 |
D | SER241 |
D | LEU242 |
D | SER243 |
D | PRO263 |
D | ILE264 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue GOL D 303 |
Chain | Residue |
D | CYS120 |
D | HIS125 |
D | CYS150 |
D | HOH410 |
D | HOH439 |
D | HOH478 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
A | ASP90 |
A | PHE91 |
D | SER51 |
D | GLU54 |
D | GLU57 |
D | HOH419 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000250 |
Chain | Residue | Details |
A | LYS155 | |
B | LYS155 | |
C | LYS155 | |
D | LYS155 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | THR43 | |
D | THR43 | |
D | TYR130 | |
D | LYS155 | |
A | TYR130 | |
A | LYS155 | |
B | THR43 | |
B | TYR130 | |
B | LYS155 | |
C | THR43 | |
C | TYR130 | |
C | LYS155 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Proton shuttle => ECO:0000250 |
Chain | Residue | Details |
A | TYR130 | |
B | TYR130 | |
C | TYR130 | |
D | TYR130 |