1RII
Crystal structure of phosphoglycerate mutase from M. Tuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004619 | molecular_function | phosphoglycerate mutase activity |
A | 0005886 | cellular_component | plasma membrane |
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 | 0032991 | cellular_component | protein-containing complex |
A | 0042802 | molecular_function | identical protein binding |
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 | 0005886 | cellular_component | plasma membrane |
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 | 0032991 | cellular_component | protein-containing complex |
B | 0042802 | molecular_function | identical protein binding |
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 | 0005886 | cellular_component | plasma membrane |
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 | 0032991 | cellular_component | protein-containing complex |
C | 0042802 | molecular_function | identical protein binding |
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 | 0005886 | cellular_component | plasma membrane |
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 | 0032991 | cellular_component | protein-containing complex |
D | 0042802 | molecular_function | identical protein binding |
D | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 501 |
Chain | Residue |
A | HIS12 |
A | SER15 |
A | ASN18 |
A | THR24 |
A | ARG63 |
A | GLU90 |
A | HOH622 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 502 |
Chain | Residue |
B | ASN18 |
B | THR24 |
B | ARG63 |
B | GLU90 |
B | HIS183 |
B | HOH607 |
B | HOH1001 |
B | HIS12 |
B | SER15 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 503 |
Chain | Residue |
D | HIS12 |
D | SER15 |
D | ASN18 |
D | THR24 |
D | ARG63 |
D | GLU90 |
D | HIS183 |
D | HOH636 |
D | HOH814 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 504 |
Chain | Residue |
D | GLN132 |
D | HOH939 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 505 |
Chain | Residue |
C | ARG83 |
D | TYR57 |
D | ARG83 |
D | VAL167 |
D | HOH888 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LlRHGEsDwN |
Chain | Residue | Details |
A | LEU9-ASN18 |
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 | HIS12 | |
B | HIS12 | |
C | HIS12 | |
D | HIS12 |
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 | GLU90 | |
B | GLU90 | |
C | GLU90 | |
D | GLU90 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:15735341 |
Chain | Residue | Details |
A | ARG11 | |
C | THR24 | |
C | ARG63 | |
C | GLU90 | |
D | ARG11 | |
D | THR24 | |
D | ARG63 | |
D | GLU90 | |
A | THR24 | |
A | ARG63 | |
A | GLU90 | |
B | ARG11 | |
B | THR24 | |
B | ARG63 | |
B | GLU90 | |
C | ARG11 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | LYS101 | |
D | LYS101 | |
D | ARG117 | |
D | GLY184 | |
A | ARG117 | |
A | GLY184 | |
B | LYS101 | |
B | ARG117 | |
B | GLY184 | |
C | LYS101 | |
C | ARG117 | |
C | GLY184 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039 |
Chain | Residue | Details |
A | HIS183 | |
B | HIS183 | |
C | HIS183 | |
D | HIS183 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
A | GLU90 | |
A | HIS183 | |
A | ARG63 | |
A | HIS12 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
B | GLU90 | |
B | HIS183 | |
B | ARG63 | |
B | HIS12 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
C | GLU90 | |
C | HIS183 | |
C | ARG63 | |
C | HIS12 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
D | GLU90 | |
D | HIS183 | |
D | ARG63 | |
D | HIS12 |