3VOV
Crystal Structure of ROK Hexokinase from Thermus thermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004396 | molecular_function | hexokinase activity |
| A | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| A | 0009384 | molecular_function | N-acylmannosamine kinase activity |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004396 | molecular_function | hexokinase activity |
| B | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| B | 0009384 | molecular_function | N-acylmannosamine kinase activity |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004396 | molecular_function | hexokinase activity |
| C | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| C | 0009384 | molecular_function | N-acylmannosamine kinase activity |
| C | 0046835 | biological_process | carbohydrate phosphorylation |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004396 | molecular_function | hexokinase activity |
| D | 0008761 | molecular_function | UDP-N-acetylglucosamine 2-epimerase activity |
| D | 0009384 | molecular_function | N-acylmannosamine kinase activity |
| D | 0046835 | biological_process | carbohydrate phosphorylation |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS159 |
| A | CYS169 |
| A | CYS171 |
| A | CYS176 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| B | PRO164 |
| A | GLN220 |
| A | ARG223 |
| A | TYR224 |
| A | ILE227 |
| A | HOH601 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS159 |
| B | CYS169 |
| B | CYS171 |
| B | CYS176 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| A | PRO164 |
| B | GLN220 |
| B | ARG223 |
| B | TYR224 |
| B | HOH611 |
| B | HOH617 |
| D | HOH594 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | ARG223 |
| B | ALA258 |
| B | GLU261 |
| B | ALA262 |
| B | ARG265 |
| B | HOH565 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | HIS159 |
| C | CYS169 |
| C | CYS171 |
| C | CYS176 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 402 |
| Chain | Residue |
| C | GLN220 |
| C | ARG223 |
| C | TYR224 |
| C | HOH586 |
| D | PRO164 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 401 |
| Chain | Residue |
| D | HIS159 |
| D | CYS169 |
| D | CYS171 |
| D | CYS176 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 402 |
| Chain | Residue |
| C | PRO164 |
| D | GLN220 |
| D | ARG223 |
| D | TYR224 |
| D | ILE227 |
| D | HOH540 |
| D | HOH594 |
Functional Information from PROSITE/UniProt
| site_id | PS01125 |
| Number of Residues | 28 |
| Details | ROK ROK family signature. VstGIGgGVvlgGrvlrGergqgGElGH |
| Chain | Residue | Details |
| A | VAL132-HIS159 |
