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1KFI

Crystal Structure of the Exocytosis-Sensitive Phosphoprotein, pp63/Parafusin (phosphoglucomutase) from Paramecium

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
A0071704biological_processorganic substance metabolic process
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
B0071704biological_processorganic substance metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 700
ChainResidue
AASP308
AASP310
AASP312
ASO4601

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AARG313
ALYS405
AZN700
ASER126
AHIS127
AASP308
AASP310
AASP312

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
ATHR23
AARG515
ASER517
AGLY518
ATHR519
AARG527

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 700
ChainResidue
BASP308
BASP310
BASP312
BSO4602

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BSER126
BHIS127
BASP308
BASP312
BARG313
BTRP375
BZN700

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
BARG515
BSER517
BGLY518
BTHR519
BARG527

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
DetailsACT_SITE: Phosphoserine intermediate
ChainResidueDetails
ASER126
BSER126

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00949
ChainResidueDetails
ATHR23
BLYS140
BTHR373
BGLU392
BLYS405
BARG527
AARG27
ALYS140
ATHR373
AGLU392
ALYS405
AARG527
BTHR23
BARG27

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: via phosphate group
ChainResidueDetails
ASER126
BSER126

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP308
AASP310
AASP312
BASP308
BASP310
BASP312

218853

PDB entries from 2024-04-24

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