4S12
1.55 Angstrom Crystal Structure of N-acetylmuramic acid 6-phosphate Etherase from Yersinia enterocolitica.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006040 | biological_process | amino sugar metabolic process |
A | 0009254 | biological_process | peptidoglycan turnover |
A | 0016803 | molecular_function | ether hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016835 | molecular_function | carbon-oxygen lyase activity |
A | 0046348 | biological_process | amino sugar catabolic process |
A | 0097173 | biological_process | N-acetylmuramic acid catabolic process |
A | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
A | 0097367 | molecular_function | carbohydrate derivative binding |
A | 1901135 | biological_process | carbohydrate derivative metabolic process |
B | 0006040 | biological_process | amino sugar metabolic process |
B | 0009254 | biological_process | peptidoglycan turnover |
B | 0016803 | molecular_function | ether hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016835 | molecular_function | carbon-oxygen lyase activity |
B | 0046348 | biological_process | amino sugar catabolic process |
B | 0097173 | biological_process | N-acetylmuramic acid catabolic process |
B | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
B | 0097367 | molecular_function | carbohydrate derivative binding |
B | 1901135 | biological_process | carbohydrate derivative metabolic process |
C | 0006040 | biological_process | amino sugar metabolic process |
C | 0009254 | biological_process | peptidoglycan turnover |
C | 0016803 | molecular_function | ether hydrolase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0016835 | molecular_function | carbon-oxygen lyase activity |
C | 0046348 | biological_process | amino sugar catabolic process |
C | 0097173 | biological_process | N-acetylmuramic acid catabolic process |
C | 0097175 | biological_process | 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process |
C | 0097367 | molecular_function | carbohydrate derivative binding |
C | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | SER73 |
A | HOH471 |
A | HOH587 |
A | ALA139 |
A | ALA140 |
A | SER141 |
A | THR144 |
A | LYS233 |
A | HOH407 |
A | HOH436 |
A | HOH449 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | ARG94 |
A | LYS218 |
A | HOH564 |
A | HOH572 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | ARG143 |
A | HOH462 |
A | HOH603 |
A | HOH628 |
A | HOH701 |
A | HOH760 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 304 |
Chain | Residue |
A | HIS287 |
A | ALA293 |
A | HOH477 |
A | HOH537 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 301 |
Chain | Residue |
B | SER73 |
B | ALA139 |
B | ALA140 |
B | SER141 |
B | THR144 |
B | HOH425 |
B | HOH501 |
B | HOH549 |
B | HOH695 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
B | PRO86 |
B | HIS92 |
B | HOH495 |
B | HOH504 |
B | HOH676 |
C | LYS108 |
C | ALA109 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 301 |
Chain | Residue |
C | ARG237 |
C | ARG240 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 302 |
Chain | Residue |
C | GLY89 |
C | VAL90 |
C | PRO91 |
C | ARG94 |
C | LYS218 |
C | HOH685 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 303 |
Chain | Residue |
A | ARG122 |
C | HIS287 |
C | HOH588 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG C 304 |
Chain | Residue |
B | HOH640 |
C | ASP19 |
C | THR20 |
C | LEU21 |
C | HOH664 |
Functional Information from PROSITE/UniProt
site_id | PS01272 |
Number of Residues | 18 |
Details | GCKR Glucokinase regulatory protein family signature. GPEaLTGSTRMKSGTaqK |
Chain | Residue | Details |
A | GLY185-LYS202 |