2F02
Crystal Structure of LacC from Enterococcus Faecalis in complex with ATP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005988 | biological_process | lactose metabolic process |
A | 0008443 | molecular_function | phosphofructokinase activity |
A | 0009024 | molecular_function | tagatose-6-phosphate kinase activity |
A | 0016301 | molecular_function | kinase activity |
A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
A | 0019512 | biological_process | lactose catabolic process via tagatose-6-phosphate |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 2001059 | biological_process | D-tagatose 6-phosphate catabolic process |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0005988 | biological_process | lactose metabolic process |
B | 0008443 | molecular_function | phosphofructokinase activity |
B | 0009024 | molecular_function | tagatose-6-phosphate kinase activity |
B | 0016301 | molecular_function | kinase activity |
B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
B | 0019512 | biological_process | lactose catabolic process via tagatose-6-phosphate |
B | 0046835 | biological_process | carbohydrate phosphorylation |
B | 2001059 | biological_process | D-tagatose 6-phosphate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ATP B 410 |
Chain | Residue |
B | LYS183 |
B | SER253 |
B | GLY254 |
B | THR257 |
B | MSE279 |
B | GLY282 |
B | MSE283 |
B | HOH418 |
B | HOH439 |
B | HOH468 |
B | HOH509 |
B | ASN185 |
B | HOH512 |
B | HOH566 |
B | HOH600 |
B | SER223 |
B | LEU224 |
B | GLY225 |
B | LYS226 |
B | GLY228 |
B | ILE242 |
B | ILE245 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ATP A 411 |
Chain | Residue |
A | LYS183 |
A | ASN185 |
A | SER223 |
A | LEU224 |
A | GLY225 |
A | GLY228 |
A | ILE242 |
A | ILE245 |
A | GLY252 |
A | SER253 |
A | GLY254 |
A | ASP255 |
A | THR257 |
A | MSE279 |
A | GLY282 |
A | MSE283 |
A | HOH448 |
A | HOH489 |
A | HOH537 |
A | HOH619 |
Functional Information from PROSITE/UniProt
site_id | PS00583 |
Number of Residues | 25 |
Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGkGlNVTrvIhDLGgdviatgvlG |
Chain | Residue | Details |
A | GLY36-GLY60 |
site_id | PS00584 |
Number of Residues | 14 |
Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. NPvGSGDatiAGLA |
Chain | Residue | Details |
A | ASN249-ALA262 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1tz3 |
Chain | Residue | Details |
A | GLY254 | |
A | ASP255 | |
A | SER253 | |
A | GLY252 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1tz3 |
Chain | Residue | Details |
B | GLY254 | |
B | ASP255 | |
B | SER253 | |
B | GLY252 |