1BQ3
SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE IN COMPLEX WITH INOSITOL HEXAKISPHOSPHATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004619 | molecular_function | phosphoglycerate mutase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005741 | cellular_component | mitochondrial outer membrane |
A | 0005758 | cellular_component | mitochondrial intermembrane space |
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 | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005741 | cellular_component | mitochondrial outer membrane |
B | 0005758 | cellular_component | mitochondrial intermembrane space |
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 | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005741 | cellular_component | mitochondrial outer membrane |
C | 0005758 | cellular_component | mitochondrial intermembrane space |
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 | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005741 | cellular_component | mitochondrial outer membrane |
D | 0005758 | cellular_component | mitochondrial intermembrane space |
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 SO4 C 300 |
Chain | Residue |
C | HIS8 |
C | SER11 |
C | ASN14 |
C | THR20 |
C | ARG59 |
C | SO4301 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 301 |
Chain | Residue |
C | TYR89 |
C | LYS97 |
C | ARG113 |
C | SO4300 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 302 |
Chain | Residue |
B | HIS8 |
B | SER11 |
B | ASN14 |
B | THR20 |
B | ARG59 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 303 |
Chain | Residue |
B | TYR89 |
B | LYS97 |
B | ARG113 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE IHP D 350 |
Chain | Residue |
D | ARG7 |
D | GLY9 |
D | SER11 |
D | TRP13 |
D | ASN14 |
D | LEU18 |
D | PHE19 |
D | THR20 |
D | TYR89 |
D | LYS97 |
D | ARG113 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE IHP A 360 |
Chain | Residue |
A | ARG7 |
A | HIS8 |
A | GLY9 |
A | SER11 |
A | TRP13 |
A | ASN14 |
A | LEU18 |
A | PHE19 |
A | THR20 |
A | TYR89 |
A | LYS97 |
A | ARG113 |
A | ARG114 |
A | ASN204 |
site_id | CAA |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
A | HIS8 |
A | HIS181 |
A | ARG7 |
A | GLU86 |
site_id | CAB |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
B | HIS8 |
B | HIS181 |
B | ARG7 |
B | GLU86 |
site_id | CAC |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
C | HIS181 |
C | ARG7 |
C | GLU86 |
C | HIS8 |
site_id | CAD |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
D | HIS8 |
D | HIS181 |
D | ARG7 |
D | GLU86 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LvRHGQsEwN |
Chain | Residue | Details |
D | LEU5-ASN14 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:10064712, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412, ECO:0000269|PubMed:9512715 |
Chain | Residue | Details |
D | HIS8 | |
C | HIS8 | |
A | HIS8 | |
B | HIS8 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10064712 |
Chain | Residue | Details |
D | GLU86 | |
C | GLU86 | |
A | GLU86 | |
B | GLU86 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412 |
Chain | Residue | Details |
D | ARG7 | |
C | ARG7 | |
A | ARG7 | |
B | ARG7 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478 |
Chain | Residue | Details |
D | THR20 | |
C | THR20 | |
A | THR20 | |
B | THR20 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10531478 |
Chain | Residue | Details |
D | ARG59 | |
C | ARG59 | |
A | ARG59 | |
B | ARG59 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:6115412 |
Chain | Residue | Details |
D | GLU86 | |
D | GLY182 | |
C | GLU86 | |
C | GLY182 | |
A | GLU86 | |
A | GLY182 | |
B | GLU86 | |
B | GLY182 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755 |
Chain | Residue | Details |
D | LYS97 | |
D | ARG113 | |
C | LYS97 | |
C | ARG113 | |
A | LYS97 | |
A | ARG113 | |
B | LYS97 | |
B | ARG113 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10064712 |
Chain | Residue | Details |
D | HIS181 | |
C | HIS181 | |
A | HIS181 | |
B | HIS181 |
site_id | SWS_FT_FI9 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
Chain | Residue | Details |
D | SER11 | |
D | SER184 | |
C | SER11 | |
C | SER184 | |
A | SER11 | |
A | SER184 | |
B | SER11 | |
B | SER184 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | TYR48 | |
C | TYR48 | |
A | TYR48 | |
B | TYR48 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | SER115 | |
C | SER115 | |
A | SER115 | |
B | SER115 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
D | SER126 | |
C | SER126 | |
A | SER126 | |
B | SER126 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | SER127 | |
C | SER127 | |
A | SER127 | |
B | SER127 |
site_id | SWS_FT_FI14 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | SER196 | |
C | SER196 | |
A | SER196 | |
B | SER196 |
site_id | SWS_FT_FI15 |
Number of Residues | 28 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
D | LYS30 | |
C | LYS56 | |
C | LYS70 | |
C | LYS138 | |
C | LYS174 | |
C | LYS190 | |
A | LYS30 | |
A | LYS56 | |
A | LYS70 | |
A | LYS138 | |
A | LYS174 | |
A | LYS190 | |
B | LYS30 | |
B | LYS56 | |
B | LYS70 | |
B | LYS138 | |
B | LYS174 | |
B | LYS190 | |
D | LYS56 | |
D | LYS70 | |
D | LYS138 | |
D | LYS174 | |
D | LYS190 | |
C | LYS30 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
D | HIS181 | |
D | HIS8 | |
D | GLU86 | |
D | ARG59 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
C | HIS181 | |
C | HIS8 | |
C | GLU86 | |
C | ARG59 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
A | HIS181 | |
A | HIS8 | |
A | GLU86 | |
A | ARG59 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
B | HIS181 | |
B | HIS8 | |
B | GLU86 | |
B | ARG59 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
D | HIS8 | covalent catalysis |
D | ARG59 | electrostatic stabiliser |
D | GLU86 | proton donor, proton shuttle (general acid/base) |
D | HIS181 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
C | HIS8 | covalent catalysis |
C | ARG59 | electrostatic stabiliser |
C | GLU86 | proton donor, proton shuttle (general acid/base) |
C | HIS181 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
A | HIS8 | covalent catalysis |
A | ARG59 | electrostatic stabiliser |
A | GLU86 | proton donor, proton shuttle (general acid/base) |
A | HIS181 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
B | HIS8 | covalent catalysis |
B | ARG59 | electrostatic stabiliser |
B | GLU86 | proton donor, proton shuttle (general acid/base) |
B | HIS181 | electrostatic stabiliser |