2YZR
Crystal structure of pyridoxine biosynthesis protein from Methanocaldococcus jannaschii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| 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 phosphate biosynthetic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| 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 phosphate biosynthetic process |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| 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 phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | GLU211 |
| C | LYS186 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 502 |
| Chain | Residue |
| A | LYS186 |
| A | HOH529 |
| C | LEU210 |
| C | GLU211 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 503 |
| Chain | Residue |
| B | ARG136 |
| B | ARG137 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 504 |
| Chain | Residue |
| C | ARG137 |
| C | ARG136 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 505 |
| Chain | Residue |
| B | LYS186 |
| B | GLU211 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 506 |
| Chain | Residue |
| A | ARG136 |
| A | ARG137 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 507 |
| Chain | Residue |
| A | LEU241 |
| A | ASN245 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 508 |
| Chain | Residue |
| C | ARG240 |
| C | LEU241 |
| C | ASN245 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 509 |
| Chain | Residue |
| B | LEU241 |
| B | ASN245 |
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 | LEU241-LEU259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Schiff-base intermediate with D-ribose 5-phosphate => ECO:0000255|HAMAP-Rule:MF_01824 |
| Chain | Residue | Details |
| A | LYS80 | |
| B | LYS80 | |
| C | LYS80 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01824 |
| Chain | Residue | Details |
| A | ASP23 | |
| B | GLY271 | |
| C | ASP23 | |
| C | GLY152 | |
| C | ARG164 | |
| C | GLY250 | |
| C | GLY271 | |
| A | GLY152 | |
| A | ARG164 | |
| A | GLY250 | |
| A | GLY271 | |
| B | ASP23 | |
| B | GLY152 | |
| B | ARG164 | |
| B | GLY250 |
