4MO5
Crystal structure of AnmK bound to AMPPCP and anhMurNAc
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 |
C | 0005524 | molecular_function | ATP binding |
C | 0006040 | biological_process | amino sugar metabolic process |
C | 0009254 | biological_process | peptidoglycan turnover |
C | 0016301 | molecular_function | kinase activity |
C | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
C | 0046677 | biological_process | response to antibiotic |
C | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
D | 0005524 | molecular_function | ATP binding |
D | 0006040 | biological_process | amino sugar metabolic process |
D | 0009254 | biological_process | peptidoglycan turnover |
D | 0016301 | molecular_function | kinase activity |
D | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
D | 0046677 | biological_process | response to antibiotic |
D | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE AH0 A 401 |
Chain | Residue |
A | THR97 |
A | HOH530 |
A | HOH534 |
A | HIS100 |
A | ARG129 |
A | ALA140 |
A | PRO141 |
A | LEU142 |
A | VAL143 |
A | GLU326 |
A | HOH528 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACP A 402 |
Chain | Residue |
A | GLY164 |
A | ASN187 |
A | ASP191 |
A | PHE202 |
A | ASP203 |
A | ARG204 |
A | ASP205 |
A | GLY292 |
A | PHE295 |
A | HOH605 |
A | HOH718 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AH0 B 401 |
Chain | Residue |
B | HIS94 |
B | THR97 |
B | HIS100 |
B | ARG129 |
B | ALA140 |
B | PRO141 |
B | LEU142 |
B | VAL143 |
B | HOH522 |
B | HOH526 |
B | HOH591 |
B | HOH617 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ACP B 402 |
Chain | Residue |
B | SER12 |
B | GLY164 |
B | GLY165 |
B | ASN187 |
B | ASP191 |
B | PHE202 |
B | ASP203 |
B | ASP205 |
B | GLY291 |
B | GLY292 |
B | PHE295 |
B | HOH518 |
B | HOH637 |
B | HOH686 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AH0 C 401 |
Chain | Residue |
C | THR11 |
C | THR97 |
C | HIS100 |
C | ARG129 |
C | ALA140 |
C | PRO141 |
C | LEU142 |
C | VAL143 |
C | HOH516 |
C | HOH544 |
C | HOH549 |
C | HOH620 |
C | HOH652 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ACP C 402 |
Chain | Residue |
C | GLY164 |
C | GLY165 |
C | ASN187 |
C | ASP191 |
C | PHE202 |
C | ASP203 |
C | ARG204 |
C | ASP205 |
C | GLY292 |
C | PHE295 |
C | HOH509 |
C | HOH556 |
C | HOH700 |
C | HOH728 |
C | HOH757 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AH0 D 401 |
Chain | Residue |
D | THR11 |
D | THR97 |
D | HIS100 |
D | ARG129 |
D | ALA140 |
D | PRO141 |
D | LEU142 |
D | VAL143 |
D | HOH528 |
D | HOH581 |
D | HOH619 |
D | HOH622 |
D | HOH754 |
site_id | AC8 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ACP D 402 |
Chain | Residue |
D | GLY292 |
D | PHE295 |
D | MG403 |
D | HOH554 |
D | HOH564 |
D | HOH595 |
D | HOH661 |
D | HOH701 |
D | HOH711 |
D | HOH757 |
D | HOH808 |
D | HOH821 |
D | SER12 |
D | ASP14 |
D | GLY164 |
D | GLY165 |
D | ASN187 |
D | ASP191 |
D | PHE202 |
D | ASP203 |
D | ARG204 |
D | ASP205 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 403 |
Chain | Residue |
D | ACP402 |
D | HOH564 |
D | HOH661 |
D | HOH701 |
D | HOH853 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01270 |
Chain | Residue | Details |
A | GLY10 | |
B | GLY10 | |
C | GLY10 | |
D | GLY10 |