4EMB
Crystal structure of a phosphoglycerate mutase gpmA from Borrelia burgdorferi B31
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004619 | molecular_function | phosphoglycerate mutase activity |
A | 0005829 | cellular_component | cytosol |
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 | 0003824 | molecular_function | catalytic activity |
B | 0004619 | molecular_function | phosphoglycerate mutase activity |
B | 0005829 | cellular_component | cytosol |
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 | 0003824 | molecular_function | catalytic activity |
C | 0004619 | molecular_function | phosphoglycerate mutase activity |
C | 0005829 | cellular_component | cytosol |
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 | 0003824 | molecular_function | catalytic activity |
D | 0004619 | molecular_function | phosphoglycerate mutase activity |
D | 0005829 | cellular_component | cytosol |
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 | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 301 |
Chain | Residue |
A | LEU24 |
A | PHE25 |
A | THR26 |
A | GLY27 |
A | GLU92 |
A | TYR95 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 301 |
Chain | Residue |
B | GLU92 |
B | TYR95 |
B | PHE25 |
B | THR26 |
B | GLY27 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 301 |
Chain | Residue |
C | LEU24 |
C | PHE25 |
C | THR26 |
C | GLY27 |
C | GLU92 |
C | TYR95 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LvRHGEsEwN |
Chain | Residue | Details |
A | LEU11-ASN20 |
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 | HIS14 | |
B | HIS14 | |
C | HIS14 | |
D | HIS14 |
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 | GLU92 | |
B | GLU92 | |
C | GLU92 | |
D | GLU92 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
B | THR26 | |
B | ARG65 | |
B | GLU92 | |
B | LYS103 | |
B | ARG119 | |
B | GLY188 | |
C | ARG13 | |
C | THR26 | |
C | ARG65 | |
C | GLU92 | |
C | LYS103 | |
C | ARG119 | |
C | GLY188 | |
D | ARG13 | |
D | THR26 | |
D | ARG65 | |
D | GLU92 | |
D | LYS103 | |
D | ARG119 | |
D | GLY188 | |
A | ARG13 | |
A | THR26 | |
A | ARG65 | |
A | GLU92 | |
A | LYS103 | |
A | ARG119 | |
A | GLY188 | |
B | ARG13 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | HIS187 | |
B | HIS187 | |
C | HIS187 | |
D | HIS187 |