6JDO
Crystal structure of N-acetyl mannosmaine kinase with AMP-PNP from Pasteurella multocida
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009384 | molecular_function | N-acylmannosamine kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009384 | molecular_function | N-acylmannosamine kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue ANP A 301 |
| Chain | Residue |
| A | SER130 |
| A | HOH428 |
| A | HOH469 |
| A | HOH480 |
| A | THR131 |
| A | GLY180 |
| A | PRO196 |
| A | LYS197 |
| A | PHE200 |
| A | SER242 |
| A | HOH402 |
| A | HOH419 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | TYR264 |
| B | CYS166 |
| B | CYS168 |
| B | GLY169 |
| B | ARG170 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 301 |
| Chain | Residue |
| A | HIS156 |
| A | CYS168 |
| A | GLY169 |
| A | ARG170 |
| B | TYR264 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue ANP B 302 |
| Chain | Residue |
| B | SER130 |
| B | THR131 |
| B | GLY180 |
| B | PRO196 |
| B | LYS197 |
| B | PHE200 |
| B | SER242 |
| B | HOH439 |
| B | HOH448 |
| B | HOH461 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01234 |
| Chain | Residue | Details |
| A | ALA5 | |
| B | CYS166 | |
| B | CYS168 | |
| B | CYS173 | |
| A | GLY132 | |
| A | HIS156 | |
| A | CYS166 | |
| A | CYS168 | |
| A | CYS173 | |
| B | ALA5 | |
| B | GLY132 | |
| B | HIS156 |
