Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016832 | molecular_function | aldehyde-lyase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 826 |
Chain | Residue |
A | ASP182 |
A | ASN215 |
A | TYR217 |
A | HTL827 |
A | HOH1251 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HTL A 827 |
Chain | Residue |
A | GLY181 |
A | ASP182 |
A | GLY183 |
A | GLU184 |
A | ASN215 |
A | TYR217 |
A | LYS218 |
A | ILE219 |
A | LYS300 |
A | HIS320 |
A | ASP436 |
A | GLU437 |
A | LEU477 |
A | GLU479 |
A | TYR501 |
A | PHE504 |
A | ASN549 |
A | HIS553 |
A | MG826 |
A | EDO836 |
A | HOH888 |
A | HOH1251 |
A | THR67 |
A | HIS97 |
A | GLY155 |
A | LEU157 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 828 |
Chain | Residue |
A | HIS480 |
A | HIS480 |
A | VAL507 |
A | VAL507 |
A | HOH870 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 829 |
Chain | Residue |
A | GLU627 |
A | ALA634 |
A | ASN636 |
A | ASN637 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 830 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 831 |
Chain | Residue |
A | GLN127 |
A | ARG131 |
A | HOH1385 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 832 |
Chain | Residue |
A | ARG524 |
A | GLU525 |
A | PHE551 |
A | GLY738 |
A | HOH1027 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 833 |
Chain | Residue |
A | THR283 |
A | LYS312 |
A | GLU314 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 834 |
Chain | Residue |
A | ALA220 |
A | TRP317 |
A | LYS452 |
A | VAL463 |
A | ASP464 |
A | GLU465 |
A | MET467 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 835 |
Chain | Residue |
A | THR566 |
A | PHE567 |
A | GLN681 |
A | ARG717 |
A | HOH1133 |
A | HOH1395 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 836 |
Chain | Residue |
A | HIS64 |
A | HIS320 |
A | GLN321 |
A | TYR501 |
A | ASN549 |
A | HTL827 |
A | PG4837 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PG4 A 837 |
Chain | Residue |
A | GLN321 |
A | SER440 |
A | ARG442 |
A | TYR501 |
A | LYS605 |
A | EDO836 |
A | HOH1178 |
A | HOH1220 |
A | HOH1222 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1397 |
Chain | Residue |
A | HIS726 |
A | HIS726 |
A | ASP727 |
A | ASP727 |
Functional Information from PROSITE/UniProt
site_id | PS60002 |
Number of Residues | 7 |
Details | PHOSPHOKETOLASE_1 Phosphoketolase signature 1. EGGELGY |
Chain | Residue | Details |
A | GLU153-TYR159 | |
site_id | PS60003 |
Number of Residues | 19 |
Details | PHOSPHOKETOLASE_2 Phosphoketolase signature 2. GavmNnPslFvpcIiGDGE |
Chain | Residue | Details |
A | GLY166-GLU184 | |