Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008478 | molecular_function | pyridoxal kinase activity |
| A | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0031402 | molecular_function | sodium ion binding |
| A | 0031403 | molecular_function | lithium ion binding |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042817 | biological_process | pyridoxal metabolic process |
| A | 0042818 | biological_process | pyridoxamine metabolic process |
| A | 0042822 | biological_process | pyridoxal phosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008478 | molecular_function | pyridoxal kinase activity |
| B | 0009443 | biological_process | pyridoxal 5'-phosphate salvage |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0031402 | molecular_function | sodium ion binding |
| B | 0031403 | molecular_function | lithium ion binding |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0035580 | cellular_component | specific granule lumen |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042816 | biological_process | vitamin B6 metabolic process |
| B | 0042817 | biological_process | pyridoxal metabolic process |
| B | 0042818 | biological_process | pyridoxamine metabolic process |
| B | 0042822 | biological_process | pyridoxal phosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | GLU153 |
| A | HOH536 |
| A | HOH537 |
| A | HOH538 |
| A | HOH539 |
| A | HOH645 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TEP A 402 |
| Chain | Residue |
| A | ASP235 |
| A | HOH546 |
| A | HOH631 |
| A | HOH633 |
| A | SER12 |
| A | GLY20 |
| A | VAL231 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 403 |
| Chain | Residue |
| A | SER12 |
| A | PHE43 |
| A | HIS46 |
| A | THR47 |
| A | HOH647 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 404 |
| Chain | Residue |
| A | THR186 |
| A | GLY234 |
| A | LEU263 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 405 |
| Chain | Residue |
| A | LYS76 |
| A | TYR77 |
| A | ASP78 |
| A | ASN105 |
| A | HOH636 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 406 |
| Chain | Residue |
| A | ILE223 |
| A | ARG224 |
| A | VAL226 |
| A | HIS264 |
| A | HOH541 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 407 |
| Chain | Residue |
| A | CYS5 |
| A | LEU31 |
| A | GLY32 |
| A | LYS247 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 408 |
| Chain | Residue |
| A | LEU156 |
| A | LYS161 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 409 |
| Chain | Residue |
| A | ARG70 |
| A | MET93 |
| A | GLU100 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 410 |
| Chain | Residue |
| A | SER40 |
| A | VAL56 |
| A | THR85 |
| A | ARG86 |
| A | ASP87 |
| A | PHE90 |
| A | HOH600 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 401 |
| Chain | Residue |
| B | GLU153 |
| B | HOH615 |
| B | HOH628 |
| B | HOH690 |
| B | HOH691 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TEP B 402 |
| Chain | Residue |
| B | SER12 |
| B | TYR84 |
| B | VAL231 |
| B | ASP235 |
| B | HOH630 |
| B | HOH660 |
| B | HOH693 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 403 |
| Chain | Residue |
| B | HIS46 |
| B | THR47 |
| B | TYR84 |
| B | MPD407 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 404 |
| Chain | Residue |
| B | ASP181 |
| B | ARG208 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MPD B 405 |
| Chain | Residue |
| B | PRO193 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 406 |
| Chain | Residue |
| B | MET126 |
| B | GLU130 |
| B | LEU156 |
| B | HOH636 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 407 |
| Chain | Residue |
| A | SER192 |
| A | PRO193 |
| B | PHE43 |
| B | TYR84 |
| B | ARG86 |
| B | MPD403 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 408 |
| Chain | Residue |
| B | THR186 |
| B | THR233 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD B 409 |
| Chain | Residue |
| B | VAL109 |
| B | THR245 |
| B | PRO249 |
| B | HOH514 |
| B | HOH572 |
| B | HOH678 |
| B | HOH684 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 410 |
| Chain | Residue |
| B | ILE223 |
| B | ARG224 |
| B | VAL226 |
| B | HIS264 |
| B | LEU267 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 411 |
| Chain | Residue |
| B | ILE223 |
| B | ARG224 |
| B | HIS264 |
| B | VAL306 |
| B | VAL307 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 412 |
| Chain | Residue |
| B | GLN63 |
| B | GLU100 |
| B | HOH689 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 413 |
| Chain | Residue |
| B | CYS5 |
| B | ASP78 |
| B | HIS246 |
| B | HOH581 |
| B | HOH663 |
| B | GLU4 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 414 |
| Chain | Residue |
| B | CYS5 |
| B | LEU31 |
| B | GLY32 |
| B | PHE33 |
| B | HIS246 |
| B | LYS247 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 415 |
| Chain | Residue |
| B | GLU155 |
| B | LEU156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:19351586 |
| Chain | Residue | Details |
| A | ASP235 | |
| B | ASP235 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0007744|PDB:3FHX |
| Chain | Residue | Details |
| A | SER12 | |
| B | SER12 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|Ref.16, ECO:0007744|PDB:3KEU |
| Chain | Residue | Details |
| A | THR47 | |
| B | THR47 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:4EN4 |
| Chain | Residue | Details |
| A | ASP113 | |
| B | ASP113 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4 |
| Chain | Residue | Details |
| A | ASP118 | |
| B | ASP118 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:2YXT, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4 |
| Chain | Residue | Details |
| A | THR148 | |
| A | THR186 | |
| B | THR148 | |
| B | THR186 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHY, ECO:0007744|PDB:3KEU |
| Chain | Residue | Details |
| A | ASN150 | |
| B | ASN150 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4 |
| Chain | Residue | Details |
| A | VAL226 | |
| B | VAL226 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16, ECO:0007744|PDB:2YXU, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3FHY, ECO:0007744|PDB:3KEU, ECO:0007744|PDB:4EN4 |
| Chain | Residue | Details |
| A | THR233 | |
| B | THR233 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19351586, ECO:0000269|Ref.16, ECO:0007744|PDB:3FHX, ECO:0007744|PDB:3KEU |
| Chain | Residue | Details |
| A | GLY234 | |
| B | GLY234 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P82197 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER59 | |
| A | SER164 | |
| B | SER59 | |
| B | SER164 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | SER213 | |
| B | SER213 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER285 | |
| B | SER285 |
