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6SNQ

Crystal structures of human PGM1 isoform 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004614molecular_functionphosphoglucomutase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0033499biological_processgalactose catabolic process via UDP-galactose
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP
ChainResidueDetails
AGLY129-PRO138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:25288802
ChainResidueDetails
ASEP135

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00949
ChainResidueDetails
AARG41
AARG311
ATHR375
AGLU394
ASER396
ALYS407

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: via phosphate groupe => ECO:0000269|PubMed:25288802
ChainResidueDetails
ASEP135

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26972339, ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C
ChainResidueDetails
AASP306
AASP308
AASP310

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS34

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
ATHR133
ATHR525

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:25288802, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASEP135

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P38652
ChainResidueDetails
ASER152
ASER231
ASER387
ASER495
ASER503
ASER559

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR203

site_idSWS_FT_FI10
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER219
ASER224
ASER396
ASER523
ASER527

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
ALYS367

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
ATYR371

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
ALYS437

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PAK1 => ECO:0000269|PubMed:15378030
ChainResidueDetails
ATHR485

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PDB entries from 2024-07-24

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