Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004618 | molecular_function | phosphoglycerate kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0020015 | cellular_component | glycosome |
A | 0043531 | molecular_function | ADP binding |
B | 0004618 | molecular_function | phosphoglycerate kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0020015 | cellular_component | glycosome |
B | 0043531 | molecular_function | ADP binding |
C | 0004618 | molecular_function | phosphoglycerate kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006096 | biological_process | glycolytic process |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0020015 | cellular_component | glycosome |
C | 0043531 | molecular_function | ADP binding |
D | 0004618 | molecular_function | phosphoglycerate kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005829 | cellular_component | cytosol |
D | 0006094 | biological_process | gluconeogenesis |
D | 0006096 | biological_process | glycolytic process |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
D | 0020015 | cellular_component | glycosome |
D | 0043531 | molecular_function | ADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 422 |
Chain | Residue |
A | ASP377 |
A | ADP421 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG B 422 |
Chain | Residue |
B | ASP377 |
B | ADP421 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 422 |
Chain | Residue |
C | ASP377 |
C | ADP421 |
C | PO4624 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG D 422 |
Chain | Residue |
D | PO4625 |
D | ASP377 |
D | ADP421 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 C 624 |
Chain | Residue |
C | ARG39 |
C | LYS219 |
C | GLY375 |
C | GLY376 |
C | GLY398 |
C | ADP421 |
C | MG422 |
C | HOH759 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 D 625 |
Chain | Residue |
D | ARG39 |
D | LYS219 |
D | GLY375 |
D | GLY376 |
D | GLY398 |
D | ADP421 |
D | MG422 |
D | HOH747 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 701 |
Chain | Residue |
A | LEU103 |
A | ARG105 |
D | PHE344 |
D | GLU345 |
D | LEU384 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 702 |
Chain | Residue |
B | LYS48 |
B | LEU103 |
C | PHE354 |
C | LEU384 |
C | HOH789 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 C 703 |
Chain | Residue |
B | PHE344 |
B | VAL347 |
B | LEU384 |
C | LEU103 |
C | ARG105 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 704 |
Chain | Residue |
A | PHE344 |
A | VAL347 |
A | LEU384 |
A | HOH789 |
D | LYS48 |
D | LEU103 |
site_id | BC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ADP A 421 |
Chain | Residue |
A | GLY217 |
A | ALA218 |
A | LYS219 |
A | LYS223 |
A | GLY241 |
A | TYR245 |
A | ALA314 |
A | LEU315 |
A | ASN338 |
A | PRO340 |
A | GLY342 |
A | VAL343 |
A | GLU345 |
A | GLY374 |
A | GLY375 |
A | GLY376 |
A | ASP377 |
A | SER378 |
A | MG422 |
A | HOH716 |
A | HOH722 |
A | HOH842 |
A | HOH861 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 3PG A 423 |
Chain | Residue |
A | ASP24 |
A | ASN26 |
A | ARG39 |
A | HIS62 |
A | ARG65 |
A | ARG135 |
A | GLY168 |
A | ARG172 |
A | LYS219 |
A | HOH724 |
A | HOH752 |
A | HOH842 |
A | HOH876 |
site_id | BC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ADP B 421 |
Chain | Residue |
B | ASP377 |
B | SER378 |
B | MG422 |
B | HOH430 |
B | HOH442 |
B | HOH556 |
B | HOH579 |
B | GLY217 |
B | ALA218 |
B | LYS219 |
B | LYS223 |
B | GLY241 |
B | ALA242 |
B | TYR245 |
B | ALA314 |
B | LEU315 |
B | ASN338 |
B | PRO340 |
B | GLY342 |
B | VAL343 |
B | GLU345 |
B | GLY375 |
B | GLY376 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 3PG B 423 |
Chain | Residue |
B | ASP24 |
B | ASN26 |
B | ARG39 |
B | HIS62 |
B | GLY64 |
B | ARG65 |
B | ARG135 |
B | GLY168 |
B | ARG172 |
B | LYS219 |
B | GLY398 |
B | HOH480 |
B | HOH556 |
site_id | BC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP C 421 |
Chain | Residue |
C | GLY217 |
C | ALA218 |
C | LYS219 |
C | LYS223 |
C | GLY241 |
C | ALA242 |
C | TYR245 |
C | ALA314 |
C | ASN338 |
C | PRO340 |
C | GLY342 |
C | VAL343 |
C | GLU345 |
C | GLY375 |
C | GLY376 |
C | ASP377 |
C | SER378 |
C | MG422 |
C | PO4624 |
site_id | BC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ADP D 421 |
Chain | Residue |
D | GLY217 |
D | ALA218 |
D | LYS219 |
D | LYS223 |
D | GLY241 |
D | ALA242 |
D | TYR245 |
D | ALA314 |
D | ASN338 |
D | GLY339 |
D | PRO340 |
D | GLY342 |
D | VAL343 |
D | GLU345 |
D | GLY375 |
D | GLY376 |
D | ASP377 |
D | SER378 |
D | MG422 |
D | PO4625 |
D | HOH654 |
Functional Information from PROSITE/UniProt
site_id | PS00111 |
Number of Residues | 11 |
Details | PGLYCERATE_KINASE Phosphoglycerate kinase signature. KVLIRvDfNVP |
Chain | Residue | Details |
A | LYS18-PRO28 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP24 | |
B | ASN338 | |
B | GLU345 | |
B | GLY375 | |
C | ASP24 | |
C | HIS62 | |
C | LYS223 | |
C | ASN338 | |
C | GLU345 | |
C | GLY375 | |
D | ASP24 | |
A | HIS62 | |
D | HIS62 | |
D | LYS223 | |
D | ASN338 | |
D | GLU345 | |
D | GLY375 | |
A | LYS223 | |
A | ASN338 | |
A | GLU345 | |
A | GLY375 | |
B | ASP24 | |
B | HIS62 | |
B | LYS223 | |
Chain | Residue | Details |
A | ARG39 | |
D | ARG39 | |
D | ARG135 | |
D | ARG172 | |
A | ARG135 | |
A | ARG172 | |
B | ARG39 | |
B | ARG135 | |
B | ARG172 | |
C | ARG39 | |
C | ARG135 | |
C | ARG172 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 9521762, 9384563 |
Chain | Residue | Details |
A | GLY376 | |
A | ARG39 | |
A | LYS219 | |
A | GLY399 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 9521762, 9384563 |
Chain | Residue | Details |
B | GLY376 | |
B | ARG39 | |
B | LYS219 | |
B | GLY399 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 9521762, 9384563 |
Chain | Residue | Details |
C | GLY376 | |
C | ARG39 | |
C | LYS219 | |
C | GLY399 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 9521762, 9384563 |
Chain | Residue | Details |
D | GLY376 | |
D | ARG39 | |
D | LYS219 | |
D | GLY399 | |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 40 |
Chain | Residue | Details |
A | ARG39 | electrostatic stabiliser, hydrogen bond donor |
A | LYS219 | electrostatic stabiliser, hydrogen bond donor |
A | GLY376 | electrostatic stabiliser, hydrogen bond donor |
A | GLY399 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 40 |
Chain | Residue | Details |
B | ARG39 | electrostatic stabiliser, hydrogen bond donor |
B | LYS219 | electrostatic stabiliser, hydrogen bond donor |
B | GLY376 | electrostatic stabiliser, hydrogen bond donor |
B | GLY399 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 40 |
Chain | Residue | Details |
C | ARG39 | electrostatic stabiliser, hydrogen bond donor |
C | LYS219 | electrostatic stabiliser, hydrogen bond donor |
C | GLY376 | electrostatic stabiliser, hydrogen bond donor |
C | GLY399 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 40 |
Chain | Residue | Details |
D | ARG39 | electrostatic stabiliser, hydrogen bond donor |
D | LYS219 | electrostatic stabiliser, hydrogen bond donor |
D | GLY376 | electrostatic stabiliser, hydrogen bond donor |
D | GLY399 | electrostatic stabiliser, hydrogen bond donor |