2DKA
Crystal structure of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, in the apo-form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004610 | molecular_function | phosphoacetylglucosamine mutase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
A | 0034221 | biological_process | obsolete fungal-type cell wall chitin biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0071555 | biological_process | cell wall organization |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004610 | molecular_function | phosphoacetylglucosamine mutase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
B | 0034221 | biological_process | obsolete fungal-type cell wall chitin biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
site_id | PS00710 |
Number of Residues | 10 |
Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmITASHNP |
Chain | Residue | Details |
A | GLY60-PRO69 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Phosphoserine intermediate => ECO:0000305|PubMed:16651269 |
Chain | Residue | Details |
A | SER66 | |
B | SER66 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: via phosphate group => ECO:0000305|PubMed:16651269 |
Chain | Residue | Details |
A | SER66 | |
B | SER66 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16651269 |
Chain | Residue | Details |
A | ASP290 | |
A | ASP292 | |
A | ASP294 | |
A | ARG521 | |
B | ASP290 | |
B | ASP292 | |
B | ASP294 | |
B | ARG521 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16651269 |
Chain | Residue | Details |
A | GLU387 | |
A | ARG512 | |
B | GLU387 | |
B | ARG512 |