3QBX
Crystal structure of pseudomonas aeruginosa 1,6-anhydro-n-actetylmuramic acid kinase (ANMK) bound to 1,6-anhydro-n-actetylmuramic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006040 | biological_process | amino sugar metabolic process |
A | 0009254 | biological_process | peptidoglycan turnover |
A | 0016301 | molecular_function | kinase activity |
A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
A | 0046677 | biological_process | response to antibiotic |
A | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
B | 0005524 | molecular_function | ATP binding |
B | 0006040 | biological_process | amino sugar metabolic process |
B | 0009254 | biological_process | peptidoglycan turnover |
B | 0016301 | molecular_function | kinase activity |
B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
B | 0046677 | biological_process | response to antibiotic |
B | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AH0 A 653 |
Chain | Residue |
A | THR97 |
A | ASP182 |
A | GLU326 |
A | HOH394 |
A | HIS100 |
A | ARG129 |
A | ALA140 |
A | PRO141 |
A | LEU142 |
A | VAL143 |
A | PHE166 |
A | ASN168 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 372 |
Chain | Residue |
A | GLY10 |
A | THR11 |
A | SER12 |
A | GLY164 |
A | GLY165 |
A | HOH412 |
A | HOH443 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AH0 B 654 |
Chain | Residue |
B | THR97 |
B | HIS100 |
B | ARG129 |
B | ALA140 |
B | PRO141 |
B | LEU142 |
B | VAL143 |
B | PHE166 |
B | ASN168 |
B | ASP182 |
B | GLU326 |
B | HOH387 |
B | HOH409 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 372 |
Chain | Residue |
B | GLY10 |
B | THR11 |
B | SER12 |
B | GLY165 |
B | HOH406 |
B | HOH409 |
B | HOH419 |
B | HOH425 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01270 |
Chain | Residue | Details |
A | GLY10 | |
B | GLY10 |