3QY9
The Crystal Structure of Dihydrodipicolinate reductase from Staphylococcus aureus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
A | 0019877 | biological_process | diaminopimelate biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
B | 0019877 | biological_process | diaminopimelate biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
C | 0009085 | biological_process | lysine biosynthetic process |
C | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
C | 0019877 | biological_process | diaminopimelate biosynthetic process |
C | 0042802 | molecular_function | identical protein binding |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
D | 0009085 | biological_process | lysine biosynthetic process |
D | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
D | 0019877 | biological_process | diaminopimelate biosynthetic process |
D | 0042802 | molecular_function | identical protein binding |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 241 |
Chain | Residue |
A | HIS136 |
A | LYS213 |
A | SO4243 |
A | HOH273 |
A | HOH423 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 242 |
Chain | Residue |
A | HOH268 |
A | HOH308 |
A | HOH505 |
A | HOH699 |
A | LYS139 |
A | SER144 |
A | GLY145 |
A | THR146 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 243 |
Chain | Residue |
A | LYS139 |
A | VAL140 |
A | ASP141 |
A | SO4241 |
A | HOH423 |
A | HOH601 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 244 |
Chain | Residue |
A | ALA10 |
A | ARG14 |
A | LYS213 |
A | HOH508 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 245 |
Chain | Residue |
A | ARG14 |
A | SER212 |
A | LYS213 |
A | HOH269 |
A | HOH590 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT B 241 |
Chain | Residue |
B | LYS138 |
B | LYS139 |
B | VAL140 |
B | ASP141 |
B | SO4245 |
B | HOH279 |
D | HOH303 |
D | HOH304 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 242 |
Chain | Residue |
B | ARG14 |
B | HOH257 |
B | HOH259 |
C | HOH284 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 243 |
Chain | Residue |
B | ALA10 |
B | ARG14 |
B | LYS213 |
B | HOH304 |
B | HOH305 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 244 |
Chain | Residue |
B | VAL164 |
B | TYR165 |
B | ASP166 |
B | LEU170 |
B | HOH478 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 245 |
Chain | Residue |
B | HIS136 |
B | LYS139 |
B | LYS213 |
B | ACT241 |
B | HOH275 |
B | HOH279 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 246 |
Chain | Residue |
B | SER103 |
B | ALA104 |
B | ASN105 |
B | HIS111 |
B | LYS149 |
B | PHE237 |
B | HOH341 |
B | HOH351 |
B | HOH443 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 247 |
Chain | Residue |
B | THR162 |
B | GLN177 |
B | HOH283 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 241 |
Chain | Residue |
B | HOH257 |
C | ARG14 |
C | SER212 |
C | HOH260 |
C | HOH262 |
C | HOH284 |
C | HOH542 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 248 |
Chain | Residue |
B | THR81 |
B | LYS139 |
B | SER144 |
B | GLY145 |
B | THR146 |
B | HOH277 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 242 |
Chain | Residue |
C | LYS139 |
C | SER144 |
C | GLY145 |
C | THR146 |
C | HOH310 |
C | HOH486 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 243 |
Chain | Residue |
C | LYS139 |
C | VAL140 |
C | ASP141 |
C | SO4244 |
C | HOH339 |
C | HOH598 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 244 |
Chain | Residue |
C | HIS136 |
C | LYS213 |
C | SO4243 |
C | HOH313 |
C | HOH339 |
C | HOH688 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 245 |
Chain | Residue |
C | ARG14 |
C | LYS213 |
C | HOH330 |
C | HOH627 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 246 |
Chain | Residue |
C | GLY9 |
C | ALA10 |
C | HOH338 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT D 241 |
Chain | Residue |
D | SER59 |
D | ASN60 |
D | PRO61 |
D | THR80 |
D | HOH321 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 242 |
Chain | Residue |
D | LYS139 |
D | SER144 |
D | GLY145 |
D | THR146 |
D | HOH257 |
D | HOH300 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 243 |
Chain | Residue |
D | HIS136 |
D | LYS139 |
D | LYS213 |
D | SO4245 |
D | HOH316 |
D | HOH502 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 244 |
Chain | Residue |
D | ARG14 |
D | LYS213 |
D | HOH342 |
D | HOH343 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 245 |
Chain | Residue |
D | LYS139 |
D | VAL140 |
D | ASP141 |
D | SO4243 |
D | HOH502 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 246 |
Chain | Residue |
D | GLY9 |
D | ALA10 |
D | HOH348 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 D 247 |
Chain | Residue |
B | ARG226 |
B | LYS230 |
D | ASN97 |
D | ASN232 |
D | HOH271 |
D | HOH621 |
D | HOH689 |
Functional Information from PROSITE/UniProt
site_id | PS01298 |
Number of Residues | 18 |
Details | DAPB Dihydrodipicolinate reductase signature. ELtEaHhnkKvDapSGTL |
Chain | Residue | Details |
A | GLU130-LEU147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
A | HIS135 | |
B | HIS135 | |
C | HIS135 | |
D | HIS135 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
A | LYS139 | |
B | LYS139 | |
C | LYS139 | |
D | LYS139 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00102 |
Chain | Residue | Details |
A | ALA79 | |
C | SER103 | |
C | HIS136 | |
C | GLY145 | |
D | ALA79 | |
D | SER103 | |
D | HIS136 | |
D | GLY145 | |
A | SER103 | |
A | HIS136 | |
A | GLY145 | |
B | ALA79 | |
B | SER103 | |
B | HIS136 | |
B | GLY145 | |
C | ALA79 |