9IX8
Crystallization and structural characterization of phosphopentomutase from the hyperthermophilic archaeon Thermococcus kodakarensis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004615 | molecular_function | phosphomannomutase activity |
A | 0008973 | molecular_function | phosphopentomutase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004615 | molecular_function | phosphomannomutase activity |
B | 0008973 | molecular_function | phosphopentomutase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004615 | molecular_function | phosphomannomutase activity |
C | 0008973 | molecular_function | phosphopentomutase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004615 | molecular_function | phosphomannomutase activity |
D | 0008973 | molecular_function | phosphopentomutase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00710 |
Number of Residues | 10 |
Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmITASHNP |
Chain | Residue | Details |
A | GLY87-PRO96 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Phosphoserine intermediate => ECO:0000250|UniProtKB:P31120 |
Chain | Residue | Details |
A | SER93 | |
B | SER93 | |
C | SER93 | |
D | SER93 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: via phosphate group => ECO:0000250 |
Chain | Residue | Details |
A | SER93 | |
B | SER93 | |
C | SER93 | |
D | SER93 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP231 | |
D | ASP231 | |
D | ASP233 | |
D | ASP235 | |
A | ASP233 | |
A | ASP235 | |
B | ASP231 | |
B | ASP233 | |
B | ASP235 | |
C | ASP231 | |
C | ASP233 | |
C | ASP235 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P31120 |
Chain | Residue | Details |
A | SER93 | |
B | SER93 | |
C | SER93 | |
D | SER93 |