4GPZ
Crystal structure of human B type phosphoglycerate mutase H11 phosphorylated form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
A | 0004619 | molecular_function | phosphoglycerate mutase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
A | 0019901 | molecular_function | protein kinase binding |
A | 0034774 | cellular_component | secretory granule lumen |
A | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
A | 0061621 | biological_process | canonical glycolysis |
A | 0070062 | cellular_component | extracellular exosome |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
B | 0003824 | molecular_function | catalytic activity |
B | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
B | 0004619 | molecular_function | phosphoglycerate mutase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
B | 0019901 | molecular_function | protein kinase binding |
B | 0034774 | cellular_component | secretory granule lumen |
B | 0046538 | molecular_function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity |
B | 0061621 | biological_process | canonical glycolysis |
B | 0070062 | cellular_component | extracellular exosome |
B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 301 |
Chain | Residue |
A | TRP68 |
A | ARG83 |
B | TRP68 |
B | ARG83 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MES A 302 |
Chain | Residue |
A | GLY24 |
A | ARG62 |
A | GLU89 |
A | TYR92 |
A | LYS100 |
A | HOH454 |
A | NEP11 |
A | ASN17 |
A | ARG21 |
A | PHE22 |
A | SER23 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MES A 303 |
Chain | Residue |
A | ALA44 |
A | ASP47 |
A | GLY234 |
A | HOH514 |
A | HOH533 |
A | HOH585 |
B | PRO125 |
B | GLU127 |
B | SER152 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsAwN |
Chain | Residue | Details |
A | LEU8-ASN17 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:23653202, ECO:0000305|PubMed:15883004 |
Chain | Residue | Details |
A | NEP11 | |
B | NEP11 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15883004 |
Chain | Residue | Details |
A | GLU89 | |
B | GLU89 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15883004, ECO:0000269|PubMed:23653202 |
Chain | Residue | Details |
A | ARG10 | |
A | SER23 | |
A | LYS100 | |
B | ARG10 | |
B | SER23 | |
B | LYS100 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q3JWH7 |
Chain | Residue | Details |
A | ARG62 | |
A | GLY187 | |
B | ARG62 | |
B | GLY187 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15883004 |
Chain | Residue | Details |
A | GLU89 | |
A | ARG116 | |
B | GLU89 | |
B | ARG116 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950 |
Chain | Residue | Details |
A | HIS186 | |
B | HIS186 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER14 | |
B | SER14 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER23 | |
B | SER23 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:23653202 |
Chain | Residue | Details |
A | TYR26 | |
B | TYR26 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER31 | |
B | SER31 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBJ1 |
Chain | Residue | Details |
A | LYS106 | |
B | LYS106 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DBJ1 |
Chain | Residue | Details |
A | SER118 | |
B | SER118 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBJ1 |
Chain | Residue | Details |
A | LYS251 | |
B | LYS251 |
site_id | SWS_FT_FI14 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22157007 |
Chain | Residue | Details |
A | LYS253 | |
A | LYS254 | |
B | LYS253 | |
B | LYS254 |