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1KFQ

Crystal Structure of Exocytosis-Sensitive Phosphoprotein, pp63/parafusin (Phosphoglucomutse) from Paramecium. OPEN FORM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004614molecular_functionphosphoglucomutase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004614molecular_functionphosphoglucomutase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 700
ChainResidue
ASER126
AASP308
AASP310
AASP312

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 700
ChainResidue
BSER126
BASP308
BASP310
BASP312

Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP
ChainResidueDetails
AGLY120-PRO129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Phosphoserine intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00949","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"via phosphate group"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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