5PGM
SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
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 |
E | 0003824 | molecular_function | catalytic activity |
E | 0004619 | molecular_function | phosphoglycerate mutase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0005739 | cellular_component | mitochondrion |
E | 0005741 | cellular_component | mitochondrial outer membrane |
E | 0005758 | cellular_component | mitochondrial intermembrane space |
E | 0005829 | cellular_component | cytosol |
E | 0006094 | biological_process | gluconeogenesis |
E | 0006096 | biological_process | glycolytic process |
E | 0016853 | molecular_function | isomerase activity |
E | 0016868 | molecular_function | intramolecular phosphotransferase activity |
E | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
F | 0003824 | molecular_function | catalytic activity |
F | 0004619 | molecular_function | phosphoglycerate mutase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0005739 | cellular_component | mitochondrion |
F | 0005741 | cellular_component | mitochondrial outer membrane |
F | 0005758 | cellular_component | mitochondrial intermembrane space |
F | 0005829 | cellular_component | cytosol |
F | 0006094 | biological_process | gluconeogenesis |
F | 0006096 | biological_process | glycolytic process |
F | 0016853 | molecular_function | isomerase activity |
F | 0016868 | molecular_function | intramolecular phosphotransferase activity |
F | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
G | 0003824 | molecular_function | catalytic activity |
G | 0004619 | molecular_function | phosphoglycerate mutase activity |
G | 0005737 | cellular_component | cytoplasm |
G | 0005739 | cellular_component | mitochondrion |
G | 0005741 | cellular_component | mitochondrial outer membrane |
G | 0005758 | cellular_component | mitochondrial intermembrane space |
G | 0005829 | cellular_component | cytosol |
G | 0006094 | biological_process | gluconeogenesis |
G | 0006096 | biological_process | glycolytic process |
G | 0016853 | molecular_function | isomerase activity |
G | 0016868 | molecular_function | intramolecular phosphotransferase activity |
G | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
H | 0003824 | molecular_function | catalytic activity |
H | 0004619 | molecular_function | phosphoglycerate mutase activity |
H | 0005737 | cellular_component | cytoplasm |
H | 0005739 | cellular_component | mitochondrion |
H | 0005741 | cellular_component | mitochondrial outer membrane |
H | 0005758 | cellular_component | mitochondrial intermembrane space |
H | 0005829 | cellular_component | cytosol |
H | 0006094 | biological_process | gluconeogenesis |
H | 0006096 | biological_process | glycolytic process |
H | 0016853 | molecular_function | isomerase activity |
H | 0016868 | molecular_function | intramolecular phosphotransferase activity |
H | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 D 300 |
Chain | Residue |
D | HIS8 |
D | SER11 |
D | ASN14 |
D | THR20 |
D | ARG59 |
D | HOH428 |
D | HOH431 |
D | HOH508 |
D | HOH549 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 301 |
Chain | Residue |
D | ARG87 |
D | TYR89 |
D | ARG113 |
D | ARG114 |
D | HOH490 |
D | HOH588 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 300 |
Chain | Residue |
C | HIS8 |
C | SER11 |
C | ASN14 |
C | THR20 |
C | ARG59 |
C | HOH555 |
C | HOH597 |
C | HOH657 |
C | HOH662 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 301 |
Chain | Residue |
C | TYR89 |
C | LYS97 |
C | ARG113 |
C | ARG114 |
C | HOH616 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 300 |
Chain | Residue |
A | SER11 |
A | ASN14 |
A | THR20 |
A | ARG59 |
A | HOH430 |
A | HOH433 |
A | HOH512 |
A | HOH555 |
A | HOH563 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | ARG87 |
A | TYR89 |
A | ARG113 |
A | ARG114 |
A | ASN183 |
A | HOH493 |
A | HOH506 |
A | HOH553 |
A | HOH603 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 300 |
Chain | Residue |
B | HIS8 |
B | SER11 |
B | ASN14 |
B | THR20 |
B | ARG59 |
B | HOH432 |
B | HOH476 |
B | HOH515 |
B | HOH578 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 301 |
Chain | Residue |
B | PHE19 |
B | TYR89 |
B | LYS97 |
B | ARG113 |
B | HOH495 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 E 300 |
Chain | Residue |
E | HOH431 |
E | HOH508 |
E | HOH549 |
E | HIS8 |
E | SER11 |
E | ASN14 |
E | THR20 |
E | ARG59 |
E | HOH428 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 301 |
Chain | Residue |
E | ARG87 |
E | TYR89 |
E | ARG113 |
E | ARG114 |
E | HOH490 |
E | HOH588 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 F 300 |
Chain | Residue |
F | HIS8 |
F | SER11 |
F | ASN14 |
F | THR20 |
F | ARG59 |
F | HOH555 |
F | HOH597 |
F | HOH657 |
F | HOH662 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 301 |
Chain | Residue |
F | TYR89 |
F | LYS97 |
F | ARG113 |
F | ARG114 |
F | HOH616 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 G 300 |
Chain | Residue |
G | SER11 |
G | ASN14 |
G | THR20 |
G | ARG59 |
G | HOH594 |
G | HOH597 |
G | HOH676 |
G | HOH719 |
G | HOH727 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 G 301 |
Chain | Residue |
G | ARG87 |
G | TYR89 |
G | ARG113 |
G | ARG114 |
G | ASN183 |
G | HOH657 |
G | HOH670 |
G | HOH717 |
G | HOH766 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 H 300 |
Chain | Residue |
H | HIS8 |
H | SER11 |
H | ASN14 |
H | THR20 |
H | ARG59 |
H | HOH432 |
H | HOH476 |
H | HOH515 |
H | HOH578 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 H 301 |
Chain | Residue |
H | PHE19 |
H | TYR89 |
H | LYS97 |
H | ARG113 |
H | HOH495 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ALA E 302 |
Chain | Residue |
E | GLU231 |
E | ALA233 |
E | ALA234 |
site_id | CIA |
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 | ARG59 |
site_id | CIB |
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 | ARG59 |
site_id | CIC |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
C | HIS181 |
C | ARG7 |
C | ARG59 |
C | HIS8 |
site_id | CID |
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 | ARG59 |
site_id | CIE |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
E | HIS8 |
E | HIS181 |
E | ARG7 |
E | ARG59 |
site_id | CIF |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
F | HIS8 |
F | HIS181 |
F | ARG7 |
F | ARG59 |
site_id | CIG |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
G | HIS8 |
G | HIS181 |
G | ARG7 |
G | ARG59 |
site_id | CIH |
Number of Residues | 4 |
Details | CATALYTIC SITE. HIS 8 PHOSPHORYLATION IS REQUIRED TO PRIME THE ENZYME. |
Chain | Residue |
H | HIS8 |
H | HIS181 |
H | ARG7 |
H | ARG59 |
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 | 8 |
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 | GLY9 | |
C | GLY9 | |
A | GLY9 | |
B | GLY9 | |
E | GLY9 | |
F | GLY9 | |
G | GLY9 | |
H | GLY9 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:10064712 |
Chain | Residue | Details |
D | ARG87 | |
C | ARG87 | |
A | ARG87 | |
B | ARG87 | |
E | ARG87 | |
F | ARG87 | |
G | ARG87 | |
H | ARG87 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478, ECO:0000269|PubMed:6115412 |
Chain | Residue | Details |
D | HIS8 | |
C | HIS8 | |
A | HIS8 | |
B | HIS8 | |
E | HIS8 | |
F | HIS8 | |
G | HIS8 | |
H | HIS8 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:10531478 |
Chain | Residue | Details |
D | GLY21 | |
C | GLY21 | |
A | GLY21 | |
B | GLY21 | |
E | GLY21 | |
F | GLY21 | |
G | GLY21 | |
H | GLY21 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10531478 |
Chain | Residue | Details |
D | ALA60 | |
C | ALA60 | |
A | ALA60 | |
B | ALA60 | |
E | ALA60 | |
F | ALA60 | |
G | ALA60 | |
H | ALA60 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755, ECO:0000269|PubMed:6115412 |
Chain | Residue | Details |
D | ARG87 | |
E | ASN183 | |
F | ARG87 | |
F | ASN183 | |
G | ARG87 | |
G | ASN183 | |
H | ARG87 | |
H | ASN183 | |
D | ASN183 | |
C | ARG87 | |
C | ASN183 | |
A | ARG87 | |
A | ASN183 | |
B | ARG87 | |
B | ASN183 | |
E | ARG87 |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10369755 |
Chain | Residue | Details |
D | ALA98 | |
E | ARG114 | |
F | ALA98 | |
F | ARG114 | |
G | ALA98 | |
G | ARG114 | |
H | ALA98 | |
H | ARG114 | |
D | ARG114 | |
C | ALA98 | |
C | ARG114 | |
A | ALA98 | |
A | ARG114 | |
B | ALA98 | |
B | ARG114 | |
E | ALA98 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10064712 |
Chain | Residue | Details |
D | GLY182 | |
C | GLY182 | |
A | GLY182 | |
B | GLY182 | |
E | GLY182 | |
F | GLY182 | |
G | GLY182 | |
H | GLY182 |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
Chain | Residue | Details |
D | GLU12 | |
E | LEU185 | |
F | GLU12 | |
F | LEU185 | |
G | GLU12 | |
G | LEU185 | |
H | GLU12 | |
H | LEU185 | |
D | LEU185 | |
C | GLU12 | |
C | LEU185 | |
A | GLU12 | |
A | LEU185 | |
B | GLU12 | |
B | LEU185 | |
E | GLU12 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | PRO49 | |
C | PRO49 | |
A | PRO49 | |
B | PRO49 | |
E | PRO49 | |
F | PRO49 | |
G | PRO49 | |
H | PRO49 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | PHE116 | |
C | PHE116 | |
A | PHE116 | |
B | PHE116 | |
E | PHE116 | |
F | PHE116 | |
G | PHE116 | |
H | PHE116 |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
D | SER127 | |
C | SER127 | |
A | SER127 | |
B | SER127 | |
E | SER127 | |
F | SER127 | |
G | SER127 | |
H | SER127 |
site_id | SWS_FT_FI13 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | PRO128 | |
C | PRO128 | |
A | PRO128 | |
B | PRO128 | |
E | PRO128 | |
F | PRO128 | |
G | PRO128 | |
H | PRO128 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
D | ASP197 | |
C | ASP197 | |
A | ASP197 | |
B | ASP197 | |
E | ASP197 | |
F | ASP197 | |
G | ASP197 | |
H | ASP197 |
site_id | SWS_FT_FI15 |
Number of Residues | 56 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
D | GLY31 | |
C | LEU57 | |
C | ALA71 | |
C | TYR139 | |
C | THR175 | |
C | HIS191 | |
A | GLY31 | |
A | LEU57 | |
A | ALA71 | |
A | TYR139 | |
A | THR175 | |
A | HIS191 | |
B | GLY31 | |
B | LEU57 | |
B | ALA71 | |
B | TYR139 | |
B | THR175 | |
B | HIS191 | |
E | GLY31 | |
D | LEU57 | |
E | LEU57 | |
E | ALA71 | |
E | TYR139 | |
E | THR175 | |
E | HIS191 | |
F | GLY31 | |
F | LEU57 | |
F | ALA71 | |
D | ALA71 | |
F | TYR139 | |
F | THR175 | |
F | HIS191 | |
G | GLY31 | |
G | LEU57 | |
G | ALA71 | |
G | TYR139 | |
G | THR175 | |
G | HIS191 | |
D | TYR139 | |
H | GLY31 | |
H | LEU57 | |
H | ALA71 | |
H | TYR139 | |
H | THR175 | |
H | HIS191 | |
D | THR175 | |
D | HIS191 | |
C | GLY31 |
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 | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
E | HIS181 | |
E | HIS8 | |
E | GLU86 | |
E | ARG59 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
F | HIS181 | |
F | HIS8 | |
F | GLU86 | |
F | ARG59 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
G | HIS181 | |
G | HIS8 | |
G | GLU86 | |
G | ARG59 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
H | HIS181 | |
H | HIS8 | |
H | GLU86 | |
H | ARG59 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
D | GLY9 | covalent catalysis |
D | ALA60 | electrostatic stabiliser |
D | ARG87 | proton donor, proton shuttle (general acid/base) |
D | GLY182 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
C | GLY9 | covalent catalysis |
C | ALA60 | electrostatic stabiliser |
C | ARG87 | proton donor, proton shuttle (general acid/base) |
C | GLY182 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
A | GLY9 | covalent catalysis |
A | ALA60 | electrostatic stabiliser |
A | ARG87 | proton donor, proton shuttle (general acid/base) |
A | GLY182 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
B | GLY9 | covalent catalysis |
B | ALA60 | electrostatic stabiliser |
B | ARG87 | proton donor, proton shuttle (general acid/base) |
B | GLY182 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
E | GLY9 | covalent catalysis |
E | ALA60 | electrostatic stabiliser |
E | ARG87 | proton donor, proton shuttle (general acid/base) |
E | GLY182 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
F | GLY9 | covalent catalysis |
F | ALA60 | electrostatic stabiliser |
F | ARG87 | proton donor, proton shuttle (general acid/base) |
F | GLY182 | electrostatic stabiliser |
site_id | MCSA7 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
G | GLY9 | covalent catalysis |
G | ALA60 | electrostatic stabiliser |
G | ARG87 | proton donor, proton shuttle (general acid/base) |
G | GLY182 | electrostatic stabiliser |
site_id | MCSA8 |
Number of Residues | 4 |
Details | M-CSA 504 |
Chain | Residue | Details |
H | GLY9 | covalent catalysis |
H | ALA60 | electrostatic stabiliser |
H | ARG87 | proton donor, proton shuttle (general acid/base) |
H | GLY182 | electrostatic stabiliser |