1TZ6
Crystal structure of aminoimidazole riboside kinase from Salmonella enterica complexed with aminoimidazole riboside and ATP analog
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006000 | biological_process | fructose metabolic process |
| A | 0008865 | molecular_function | fructokinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006000 | biological_process | fructose metabolic process |
| B | 0008865 | molecular_function | fructokinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ACP401 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 404 |
| Chain | Residue |
| A | ASP246 |
| A | THR248 |
| A | ALA287 |
| A | ALA290 |
| A | GLY292 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 405 |
| Chain | Residue |
| A | GLY213 |
| A | ALA180 |
| A | ALA181 |
| A | ALA183 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 503 |
| Chain | Residue |
| B | ACP501 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 504 |
| Chain | Residue |
| B | ALA180 |
| B | ALA181 |
| B | ALA183 |
| B | GLY213 |
| B | HOH525 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K B 505 |
| Chain | Residue |
| B | ASP246 |
| B | THR248 |
| B | ALA287 |
| B | GLY292 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ACP A 401 |
| Chain | Residue |
| A | ASP158 |
| A | VAL159 |
| A | ASN160 |
| A | LYS187 |
| A | GLU192 |
| A | SER220 |
| A | GLY222 |
| A | ALA223 |
| A | GLY225 |
| A | PRO240 |
| A | VAL244 |
| A | ALA250 |
| A | GLY251 |
| A | ASN281 |
| A | GLY284 |
| A | ALA285 |
| A | MG403 |
| A | HOH410 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AIS A 402 |
| Chain | Residue |
| A | ASP12 |
| A | SER14 |
| A | ASP16 |
| A | GLY31 |
| A | ASN35 |
| A | LEU87 |
| A | TYR101 |
| A | ARG162 |
| A | MET165 |
| A | ASP252 |
| A | ALA293 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ACP B 501 |
| Chain | Residue |
| B | ASN160 |
| B | LYS187 |
| B | SER189 |
| B | GLU192 |
| B | SER220 |
| B | GLY222 |
| B | ALA223 |
| B | GLY225 |
| B | PRO240 |
| B | VAL244 |
| B | GLY251 |
| B | PHE254 |
| B | ASN281 |
| B | MG503 |
| B | HOH508 |
Functional Information from PROSITE/UniProt
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDafvGGLL |
| Chain | Residue | Details |
| A | ASP246-LEU259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TZ3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TZ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15458630","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TZ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TZ6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | ASP252 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | ASP252 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| A | GLY249 | |
| A | GLY251 | |
| A | ASP252 | |
| A | ALA250 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1lio |
| Chain | Residue | Details |
| B | GLY249 | |
| B | GLY251 | |
| B | ASP252 | |
| B | ALA250 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 751 |
| Chain | Residue | Details |
| A | GLY249 | electrostatic stabiliser |
| A | ALA250 | electrostatic stabiliser |
| A | GLY251 | electrostatic stabiliser |
| A | ASP252 | electrostatic stabiliser, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 751 |
| Chain | Residue | Details |
| B | GLY249 | electrostatic stabiliser |
| B | ALA250 | electrostatic stabiliser |
| B | GLY251 | electrostatic stabiliser |
| B | ASP252 | electrostatic stabiliser, proton shuttle (general acid/base) |
