1XAI
CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 600 |
| Chain | Residue |
| A | GLU178 |
| A | HIS242 |
| A | HIS256 |
| A | CRB500 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 601 |
| Chain | Residue |
| B | ASP130 |
| B | GLU178 |
| B | HIS242 |
| B | HIS256 |
| B | CRB501 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CRB A 500 |
| Chain | Residue |
| A | ASP130 |
| A | LYS136 |
| A | ASN146 |
| A | GLU178 |
| A | LYS181 |
| A | LYS221 |
| A | ARG235 |
| A | LEU238 |
| A | ASN239 |
| A | HIS242 |
| A | HIS246 |
| A | HIS256 |
| A | LYS314 |
| A | ZN600 |
| B | ARG115 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CRB B 501 |
| Chain | Residue |
| A | ARG115 |
| B | ASP130 |
| B | LYS136 |
| B | ASN146 |
| B | GLU178 |
| B | LYS181 |
| B | LYS221 |
| B | ARG235 |
| B | LEU238 |
| B | ASN239 |
| B | HIS242 |
| B | HIS246 |
| B | HIS256 |
| B | LYS314 |
| B | ZN601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL |
| Chain | Residue | Details |
| A | ASP39 | |
| A | GLU68 | |
| B | ASP39 | |
| B | GLU68 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAL |
| Chain | Residue | Details |
| A | TYR45 | |
| B | TYR45 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAH, ECO:0007744|PDB:1XAJ, ECO:0007744|PDB:1XAL |
| Chain | Residue | Details |
| A | GLY100 | |
| B | PHE163 | |
| A | THR124 | |
| A | LYS136 | |
| A | LYS145 | |
| A | PHE163 | |
| B | GLY100 | |
| B | THR124 | |
| B | LYS136 | |
| B | LYS145 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:15465043, ECO:0007744|PDB:1XAI |
| Chain | Residue | Details |
| A | GLU178 | |
| A | HIS242 | |
| A | HIS256 | |
| B | GLU178 | |
| B | HIS242 | |
| B | HIS256 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS246 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| B | HIS246 |
