3DI1
Crystal structure of the Staphylococcus aureus Dihydrodipicolinate synthase-pyruvate complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
A | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0009436 | biological_process | glyoxylate catabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0019877 | biological_process | diaminopimelate biosynthetic process |
A | 0044281 | biological_process | small molecule metabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008700 | molecular_function | 4-hydroxy-2-oxoglutarate aldolase activity |
B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0009436 | biological_process | glyoxylate catabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0019877 | biological_process | diaminopimelate biosynthetic process |
B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PYR A 1001 |
Chain | Residue |
A | ALA11 |
A | GLY45 |
A | THR46 |
A | THR47 |
A | MET103 |
A | TYR135 |
A | LYS163 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PYR B 1002 |
Chain | Residue |
B | THR46 |
B | THR47 |
B | TYR135 |
B | LYS163 |
B | ALA11 |
B | GLY45 |
Functional Information from PROSITE/UniProt
site_id | PS00666 |
Number of Residues | 31 |
Details | DHDPS_2 Dihydrodipicolinate synthase signature 2. YNVPsrTnmtIepetveilsqhpy.IvALKDA |
Chain | Residue | Details |
A | TYR135-ALA165 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:18671976 |
Chain | Residue | Details |
A | TYR135 | |
B | TYR135 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:18671976 |
Chain | Residue | Details |
A | LYS163 | |
B | LYS163 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:18671976 |
Chain | Residue | Details |
A | THR47 | |
B | THR47 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418 |
Chain | Residue | Details |
A | ILE206 | |
B | ILE206 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Part of a proton relay during catalysis => ECO:0000305 |
Chain | Residue | Details |
A | THR46 | |
A | TYR109 | |
B | THR46 | |
B | TYR109 |