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2F7L

Crystal structure of Sulfolobus tokodaii phosphomannomutase/phosphoglucomutase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005975biological_processcarbohydrate metabolic process
A0008966molecular_functionphosphoglucosamine mutase activity
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005975biological_processcarbohydrate metabolic process
B0008966molecular_functionphosphoglucosamine mutase activity
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 460
ChainResidue
AARG421
ASER423
AGLY424
ATHR425
AARG430

Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVvITASHNP
ChainResidueDetails
AGLY91-PRO100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000250|UniProtKB:P31120
ChainResidueDetails
ASER97
BSER97

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: via phosphate group => ECO:0000250|UniProtKB:P00949
ChainResidueDetails
ASER97
BSER97

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00949
ChainResidueDetails
AASP241
AASP243
AASP245
BASP241
BASP243
BASP245

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P31120
ChainResidueDetails
ASER97
BSER97

222926

PDB entries from 2024-07-24

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