3O05
Crystal Structure of Yeast Pyridoxal 5-Phosphate Synthase Snz1 Complxed with Substrate PLP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006543 | biological_process | L-glutamine catabolic process |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0016843 | molecular_function | amine-lyase activity |
| A | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| A | 0042819 | biological_process | vitamin B6 biosynthetic process |
| A | 0042823 | biological_process | pyridoxal 5'-phosphate biosynthetic process |
| A | 1903600 | cellular_component | glutaminase complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0006543 | biological_process | L-glutamine catabolic process |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0016843 | molecular_function | amine-lyase activity |
| B | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| B | 0042819 | biological_process | vitamin B6 biosynthetic process |
| B | 0042823 | biological_process | pyridoxal 5'-phosphate biosynthetic process |
| B | 1903600 | cellular_component | glutaminase complex |
| C | 0005515 | molecular_function | protein binding |
| C | 0006543 | biological_process | L-glutamine catabolic process |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0016843 | molecular_function | amine-lyase activity |
| C | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| C | 0042819 | biological_process | vitamin B6 biosynthetic process |
| C | 0042823 | biological_process | pyridoxal 5'-phosphate biosynthetic process |
| C | 1903600 | cellular_component | glutaminase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP A 1 |
| Chain | Residue |
| A | GLU104 |
| A | HOH404 |
| A | TRP111 |
| A | HIS114 |
| A | ARG136 |
| A | ARG137 |
| A | LYS148 |
| A | ARG190 |
| A | HOH335 |
| A | HOH384 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1 |
| Chain | Residue |
| B | ILE83 |
| B | GLU104 |
| B | TRP111 |
| B | HIS114 |
| B | LYS129 |
| B | GLU133 |
| B | ARG136 |
| B | ARG137 |
| B | LYS148 |
| B | HOH309 |
| B | HOH354 |
| B | HOH371 |
| B | HOH373 |
| B | HOH379 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 1 |
| Chain | Residue |
| C | GLU104 |
| C | TRP111 |
| C | HIS114 |
| C | LYS129 |
| C | GLU133 |
| C | ARG136 |
| C | ARG137 |
| C | LYS148 |
| C | HOH351 |
| C | HOH353 |
| C | HOH361 |
| C | HOH391 |
Functional Information from PROSITE/UniProt
| site_id | PS01235 |
| Number of Residues | 19 |
| Details | PDXS_SNZ_1 PdxS/SNZ family signature. LPVVNFAAGGVATPADAAL |
| Chain | Residue | Details |
| A | LEU205-LEU223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Schiff-base intermediate with D-ribose 5-phosphate","evidences":[{"source":"UniProtKB","id":"O59080","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O59080","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20919991","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
