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9IX8

Crystallization and structural characterization of phosphopentomutase from the hyperthermophilic archaeon Thermococcus kodakarensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004615molecular_functionphosphomannomutase activity
A0008973molecular_functionphosphopentomutase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
B0004615molecular_functionphosphomannomutase activity
B0008973molecular_functionphosphopentomutase activity
B0016853molecular_functionisomerase activity
B0046872molecular_functionmetal ion binding
C0004615molecular_functionphosphomannomutase activity
C0008973molecular_functionphosphopentomutase activity
C0016853molecular_functionisomerase activity
C0046872molecular_functionmetal ion binding
D0004615molecular_functionphosphomannomutase activity
D0008973molecular_functionphosphopentomutase activity
D0016853molecular_functionisomerase activity
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmITASHNP
ChainResidueDetails
AGLY87-PRO96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000250|UniProtKB:P31120
ChainResidueDetails
ASER93
BSER93
CSER93
DSER93

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: via phosphate group => ECO:0000250
ChainResidueDetails
ASER93
BSER93
CSER93
DSER93

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP231
DASP231
DASP233
DASP235
AASP233
AASP235
BASP231
BASP233
BASP235
CASP231
CASP233
CASP235

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P31120
ChainResidueDetails
ASER93
BSER93
CSER93
DSER93

234785

PDB entries from 2025-04-16

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