5UM0
Crystal structure of 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Neisseria gonorrhoeae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004619 | molecular_function | phosphoglycerate mutase activity |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
A | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
B | 0004619 | molecular_function | phosphoglycerate mutase activity |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
B | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
C | 0004619 | molecular_function | phosphoglycerate mutase activity |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006096 | biological_process | glycolytic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0016868 | molecular_function | intramolecular phosphotransferase activity |
C | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
D | 0004619 | molecular_function | phosphoglycerate mutase activity |
D | 0006094 | biological_process | gluconeogenesis |
D | 0006096 | biological_process | glycolytic process |
D | 0016853 | molecular_function | isomerase activity |
D | 0016868 | molecular_function | intramolecular phosphotransferase activity |
D | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue TLA A 300 |
Chain | Residue |
A | ARG7 |
A | HOH403 |
A | HOH409 |
A | HOH423 |
A | HOH442 |
A | HOH447 |
A | HOH459 |
A | HOH528 |
A | HOH554 |
A | ASN14 |
A | LEU18 |
A | PHE19 |
A | THR20 |
A | GLY21 |
A | GLU86 |
A | TYR89 |
A | LYS97 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue TLA B 300 |
Chain | Residue |
B | ARG7 |
B | PHE19 |
B | THR20 |
B | GLY21 |
B | GLU86 |
B | LYS97 |
B | ASN183 |
B | HOH454 |
B | HOH457 |
B | HOH473 |
B | HOH529 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue TLA C 300 |
Chain | Residue |
C | ARG7 |
C | ASN14 |
C | LEU18 |
C | PHE19 |
C | THR20 |
C | GLY21 |
C | GLU86 |
C | TYR89 |
C | LYS97 |
C | ASN183 |
C | HOH403 |
C | HOH424 |
C | HOH447 |
C | HOH450 |
C | HOH504 |
C | HOH518 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue TLA D 300 |
Chain | Residue |
D | ARG7 |
D | PHE19 |
D | THR20 |
D | GLY21 |
D | GLU86 |
D | TYR89 |
D | LYS97 |
D | ARG113 |
D | HOH411 |
D | HOH416 |
D | HOH418 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | HIS8 | |
B | HIS8 | |
C | HIS8 | |
D | HIS8 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | GLU86 | |
B | GLU86 | |
C | GLU86 | |
D | GLU86 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | ARG7 | |
B | ARG59 | |
B | GLU86 | |
B | LYS97 | |
B | ARG113 | |
B | GLY182 | |
C | ARG7 | |
C | THR20 | |
C | ARG59 | |
C | GLU86 | |
C | LYS97 | |
A | THR20 | |
C | ARG113 | |
C | GLY182 | |
D | ARG7 | |
D | THR20 | |
D | ARG59 | |
D | GLU86 | |
D | LYS97 | |
D | ARG113 | |
D | GLY182 | |
A | ARG59 | |
A | GLU86 | |
A | LYS97 | |
A | ARG113 | |
A | GLY182 | |
B | ARG7 | |
B | THR20 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | HIS181 | |
B | HIS181 | |
C | HIS181 | |
D | HIS181 |