1XUP
ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0004370 | molecular_function | glycerol kinase activity |
O | 0005524 | molecular_function | ATP binding |
O | 0005975 | biological_process | carbohydrate metabolic process |
O | 0006071 | biological_process | glycerol metabolic process |
O | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
O | 0016301 | molecular_function | kinase activity |
O | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
O | 0019563 | biological_process | glycerol catabolic process |
X | 0004370 | molecular_function | glycerol kinase activity |
X | 0005524 | molecular_function | ATP binding |
X | 0005975 | biological_process | carbohydrate metabolic process |
X | 0006071 | biological_process | glycerol metabolic process |
X | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
X | 0016301 | molecular_function | kinase activity |
X | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
X | 0019563 | biological_process | glycerol catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL O 500 |
Chain | Residue |
O | ARG84 |
O | GLU85 |
O | TRP104 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL X 501 |
Chain | Residue |
X | GLN247 |
X | PHE271 |
X | GLN83 |
X | ARG84 |
X | GLU85 |
X | TRP104 |
X | TYR136 |
X | ASP246 |
Functional Information from PROSITE/UniProt
site_id | PS00445 |
Number of Residues | 21 |
Details | FGGY_KINASES_2 FGGY family of carbohydrate kinases signature 2. GaVFGLtrgttke.DFVRATLQ |
Chain | Residue | Details |
O | GLY363-GLN383 |
site_id | PS00933 |
Number of Residues | 13 |
Details | FGGY_KINASES_1 FGGY family of carbohydrate kinases signature 1. YfSatKVRWLLDN |
Chain | Residue | Details |
O | TYR136-ASN148 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 26 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00186 |
Chain | Residue | Details |
O | THR15 | |
O | SER312 | |
O | TRP316 | |
O | ALA413 | |
O | ASP417 | |
X | THR15 | |
X | SER16 | |
X | SER17 | |
X | ALA19 | |
X | GLU85 | |
X | THR86 | |
O | SER16 | |
X | PHE137 | |
X | GLN247 | |
X | GLY269 | |
X | SER312 | |
X | TRP316 | |
X | ALA413 | |
X | ASP417 | |
O | SER17 | |
O | ALA19 | |
O | GLU85 | |
O | THR86 | |
O | PHE137 | |
O | GLN247 | |
O | GLY269 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:19102629, ECO:0007744|PDB:3D7E |
Chain | Residue | Details |
O | GLN248 | |
X | GLN248 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphohistidine; by HPr => ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:9162046 |
Chain | Residue | Details |
O | PHE233 | |
X | PHE233 |