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 |