3GP3
Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0003824 | molecular_function | catalytic 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 | 0003824 | molecular_function | catalytic 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 | 0003824 | molecular_function | catalytic 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 | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 A 250 |
| Chain | Residue |
| A | ASP51 |
| A | ALA173 |
| A | LYS175 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO3 A 251 |
| Chain | Residue |
| A | GLY183 |
| A | SEP252 |
| A | HOH274 |
| A | ARG8 |
| A | HIS9 |
| A | ASN15 |
| A | ARG60 |
| A | GLU87 |
| A | HIS182 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SEP A 252 |
| Chain | Residue |
| A | ARG8 |
| A | ASN15 |
| A | ARG19 |
| A | THR21 |
| A | GLY22 |
| A | GLU87 |
| A | ARG88 |
| A | TYR90 |
| A | LYS98 |
| A | ARG114 |
| A | ARG115 |
| A | ASN184 |
| A | PO3251 |
| A | HOH278 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 250 |
| Chain | Residue |
| B | ASP51 |
| B | ALA173 |
| B | LYS175 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO3 B 251 |
| Chain | Residue |
| B | ARG8 |
| B | HIS9 |
| B | ASN15 |
| B | ARG60 |
| B | GLU87 |
| B | HIS182 |
| B | GLY183 |
| B | SEP252 |
| B | HOH279 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SEP B 252 |
| Chain | Residue |
| B | ARG8 |
| B | ASN15 |
| B | ARG19 |
| B | THR21 |
| B | GLY22 |
| B | GLU87 |
| B | TYR90 |
| B | LYS98 |
| B | ARG114 |
| B | ARG115 |
| B | ASN184 |
| B | PO3251 |
| B | HOH299 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 C 250 |
| Chain | Residue |
| C | ASP51 |
| C | ALA173 |
| C | LYS175 |
| C | HOH552 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 C 251 |
| Chain | Residue |
| C | ILE196 |
| C | LEU204 |
| C | HIS225 |
| C | HOH332 |
| C | HOH556 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO3 C 252 |
| Chain | Residue |
| C | ARG8 |
| C | HIS9 |
| C | ASN15 |
| C | ARG60 |
| C | GLU87 |
| C | HIS182 |
| C | GLY183 |
| C | SEP253 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SEP C 253 |
| Chain | Residue |
| C | ARG8 |
| C | ASN15 |
| C | ARG19 |
| C | PHE20 |
| C | THR21 |
| C | GLY22 |
| C | GLU87 |
| C | TYR90 |
| C | LYS98 |
| C | ARG114 |
| C | ARG115 |
| C | ASN184 |
| C | PO3252 |
| C | HOH305 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 D 250 |
| Chain | Residue |
| D | ASP51 |
| D | ALA173 |
| D | LYS175 |
| D | HOH601 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 D 251 |
| Chain | Residue |
| D | ILE190 |
| D | ILE196 |
| D | TYR214 |
| D | HIS225 |
| D | TYR227 |
| D | HOH282 |
| D | HOH374 |
| D | HOH706 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO3 D 252 |
| Chain | Residue |
| D | HIS182 |
| D | GLY183 |
| D | SEP253 |
| D | HOH290 |
| D | ARG8 |
| D | HIS9 |
| D | ASN15 |
| D | ARG60 |
| D | GLU87 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SEP D 253 |
| Chain | Residue |
| D | ARG8 |
| D | ASN15 |
| D | ARG19 |
| D | PHE20 |
| D | THR21 |
| D | GLY22 |
| D | GLU87 |
| D | TYR90 |
| D | LYS98 |
| D | ARG114 |
| D | ARG115 |
| D | ASN184 |
| D | PO3252 |
| D | HOH295 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN |
| Chain | Residue | Details |
| A | LEU6-ASN15 |
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, ECO:0000269|PubMed:21904048 |
| Chain | Residue | Details |
| A | HIS9 | |
| B | HIS9 | |
| C | HIS9 | |
| D | HIS9 |
| 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 | GLU87 | |
| B | GLU87 | |
| C | GLU87 | |
| D | GLU87 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 56 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21904048, ECO:0007744|PDB:3FDZ |
| Chain | Residue | Details |
| A | ARG8 | |
| B | ARG60 | |
| B | GLU87 | |
| B | LYS98 | |
| B | ARG114 | |
| B | GLY183 | |
| C | ARG8 | |
| C | THR21 | |
| C | ARG60 | |
| C | GLU87 | |
| C | LYS98 | |
| A | THR21 | |
| C | ARG114 | |
| C | GLY183 | |
| D | ARG8 | |
| D | THR21 | |
| D | ARG60 | |
| D | GLU87 | |
| D | LYS98 | |
| D | ARG114 | |
| D | GLY183 | |
| A | HIS9 | |
| A | ARG60 | |
| A | ASN15 | |
| A | GLY22 | |
| A | TYR90 | |
| A | ARG115 | |
| A | HIS182 | |
| A | ASN184 | |
| B | HIS9 | |
| B | ASN15 | |
| B | GLY22 | |
| B | TYR90 | |
| A | GLU87 | |
| B | ARG115 | |
| B | HIS182 | |
| B | ASN184 | |
| C | HIS9 | |
| C | ASN15 | |
| C | GLY22 | |
| C | TYR90 | |
| C | ARG115 | |
| C | HIS182 | |
| C | ASN184 | |
| A | LYS98 | |
| D | HIS9 | |
| D | ASN15 | |
| D | GLY22 | |
| D | TYR90 | |
| D | ARG115 | |
| D | HIS182 | |
| D | ASN184 | |
| A | ARG114 | |
| A | GLY183 | |
| B | ARG8 | |
| B | THR21 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039 |
| Chain | Residue | Details |
| A | HIS182 | |
| B | HIS182 | |
| C | HIS182 | |
| D | HIS182 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | HIS182 | |
| A | ARG60 | |
| A | GLU87 | |
| A | HIS9 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| B | HIS182 | |
| B | ARG60 | |
| B | GLU87 | |
| B | HIS9 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| C | HIS182 | |
| C | ARG60 | |
| C | GLU87 | |
| C | HIS9 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| D | HIS182 | |
| D | ARG60 | |
| D | GLU87 | |
| D | HIS9 |
