1YGJ
Crystal Structure of Pyridoxal Kinase in Complex with Roscovitine and Derivatives
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008478 | molecular_function | pyridoxal kinase activity |
| A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| A | 0016301 | molecular_function | kinase activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RMC A 1001 |
| Chain | Residue |
| A | SER12 |
| A | HIS163 |
| A | GLY232 |
| A | ASP235 |
| A | VAL14 |
| A | VAL19 |
| A | GLY20 |
| A | PHE43 |
| A | HIS46 |
| A | THR47 |
| A | TYR84 |
| A | TYR127 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O00764 |
| Chain | Residue | Details |
| A | ASP235 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFT |
| Chain | Residue | Details |
| A | SER12 | |
| A | THR47 | |
| A | ASP235 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR, ECO:0007744|PDB:1RFT |
| Chain | Residue | Details |
| A | ASP113 | |
| A | THR148 | |
| A | THR186 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFU |
| Chain | Residue | Details |
| A | TYR127 | |
| A | GLY232 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR |
| Chain | Residue | Details |
| A | ASN150 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12235162, ECO:0007744|PDB:1LHR |
| Chain | Residue | Details |
| A | MET223 | |
| A | THR233 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:10395444 |
| Chain | Residue | Details |
| A | MET1 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00764 |
| Chain | Residue | Details |
| A | SER59 | |
| A | SER164 | |
| A | SER213 | |
| A | SER285 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1tz3 |
| Chain | Residue | Details |
| A | GLY234 | |
| A | THR233 | |
| A | GLY232 | |
| A | ASP235 |
