1TRK
REFINED STRUCTURE OF TRANSKETOLASE FROM SACCHAROMYCES CEREVISIAE AT 2.0 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004802 | molecular_function | transketolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004802 | molecular_function | transketolase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 681 |
| Chain | Residue |
| A | ASP157 |
| A | ASN187 |
| A | ILE189 |
| A | TPP682 |
| A | HOH683 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 681 |
| Chain | Residue |
| B | HOH1064 |
| B | ASP157 |
| B | ASN187 |
| B | ILE189 |
| B | TPP682 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP A 682 |
| Chain | Residue |
| A | ALA33 |
| A | HIS69 |
| A | GLY116 |
| A | PRO117 |
| A | LEU118 |
| A | ASP157 |
| A | GLY158 |
| A | GLU162 |
| A | ASN187 |
| A | ILE189 |
| A | THR190 |
| A | ILE191 |
| A | ILE250 |
| A | HIS263 |
| A | CA681 |
| A | HOH683 |
| A | HOH684 |
| A | HOH686 |
| A | HOH687 |
| B | ASP382 |
| B | GLU418 |
| B | PHE445 |
| B | TYR448 |
| B | HIS481 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP B 682 |
| Chain | Residue |
| A | ASP382 |
| A | GLU418 |
| A | PHE445 |
| A | TYR448 |
| A | HIS481 |
| B | ALA33 |
| B | HIS69 |
| B | GLY116 |
| B | PRO117 |
| B | LEU118 |
| B | ASP157 |
| B | GLY158 |
| B | GLU162 |
| B | ASN187 |
| B | ILE189 |
| B | THR190 |
| B | ILE191 |
| B | ILE250 |
| B | HIS263 |
| B | CA681 |
| B | HOH1063 |
| B | HOH1064 |
| B | HOH1065 |
| B | HOH1066 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8176731","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8999873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398292","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"9398292","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| B | HIS30 | |
| B | HIS263 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| A | HIS30 | |
| A | HIS263 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 219 |
| Chain | Residue | Details |
| A | HIS30 | activator, hydrogen bond donor, steric role |
| A | HIS263 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU418 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS481 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 219 |
| Chain | Residue | Details |
| B | HIS30 | activator, hydrogen bond donor, steric role |
| B | HIS263 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU418 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS481 | electrostatic stabiliser, hydrogen bond acceptor |
