2ECP
THE CRYSTAL STRUCTURE OF THE E. COLI MALTODEXTRIN PHOSPHORYLASE COMPLEX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005980 | biological_process | glycogen catabolic process |
| A | 0008184 | molecular_function | glycogen phosphorylase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030980 | biological_process | alpha-glucan catabolic process |
| A | 0031220 | molecular_function | maltodextrin phosphorylase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0102250 | molecular_function | obsolete linear malto-oligosaccharide phosphorylase activity |
| A | 0102499 | molecular_function | obsolete SHG alpha-glucan phosphorylase activity |
| B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005980 | biological_process | glycogen catabolic process |
| B | 0008184 | molecular_function | glycogen phosphorylase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030980 | biological_process | alpha-glucan catabolic process |
| B | 0031220 | molecular_function | maltodextrin phosphorylase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0102250 | molecular_function | obsolete linear malto-oligosaccharide phosphorylase activity |
| B | 0102499 | molecular_function | obsolete SHG alpha-glucan phosphorylase activity |
Functional Information from PDB Data
| site_id | CAT |
| Number of Residues | 1 |
| Details | CATALYTIC SITE LYSINE TO WHICH PLP COFACTOR ATTACHED (CATALYTIC SITE IS SUB-SITE -1) |
| Chain | Residue |
| A | LYS680 |
| site_id | CBT |
| Number of Residues | 1 |
| Details | CATALYTIC SITE LYSINE TO WHICH PLP COFACTOR ATTACHED (CATALYTIC SITE IS SUB-SITE -1) |
| Chain | Residue |
| B | LYS680 |
| site_id | OLA |
| Number of Residues | 2 |
| Details | CONSERVED TYROSINES THAT FORM SUB-SITES 2 AND 4 OF SUBSTRATE BINDING SITE. THE SCISSILE GLYCOSIDIC BOND WOULD SPAN SUB-SITES -1 TO +1. |
| Chain | Residue |
| A | TYR280 |
| A | TYR613 |
| site_id | OLB |
| Number of Residues | 2 |
| Details | CONSERVED TYROSINES THAT FORM SUB-SITES 2 AND 4 OF SUBSTRATE BINDING SITE. THE SCISSILE GLYCOSIDIC BOND WOULD SPAN SUB-SITES -1 TO +1. |
| Chain | Residue |
| B | TYR280 |
| B | TYR613 |
Functional Information from PROSITE/UniProt
| site_id | PS00102 |
| Number of Residues | 13 |
| Details | PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKlaLN |
| Chain | Residue | Details |
| A | GLU672-ASN684 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LEU275 | |
| B | LEU275 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LEU681 | |
| B | LEU681 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gpa |
| Chain | Residue | Details |
| A | ARG569 | |
| A | LYS568 | |
| A | THR676 | |
| A | LYS574 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gpa |
| Chain | Residue | Details |
| B | ARG569 | |
| B | LYS568 | |
| B | THR676 | |
| B | LYS574 |
