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6UIQ

Crystal structure of wild-type human phosphoglucomutase 1 in complex with Glucose-6-Phosphate

Replaces:  6BJ0
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
A0071704biological_processobsolete organic substance metabolic process
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0000287molecular_functionmagnesium ion binding
B0004614molecular_functionphosphoglucomutase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006006biological_processglucose metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0033499biological_processgalactose catabolic process via UDP-galactose
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0071704biological_processobsolete organic substance metabolic process
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP
ChainResidueDetails
BGLY111-PRO120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:25288802
ChainResidueDetails
BSER117
ASER117

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00949
ChainResidueDetails
BARG23
AGLU376
ASER378
ALYS389
BARG293
BTHR357
BGLU376
BSER378
BLYS389
AARG23
AARG293
ATHR357

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: via phosphate groupe => ECO:0000269|PubMed:25288802
ChainResidueDetails
BSER117
ASER117

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:26972339, ECO:0007744|PDB:5EPC, ECO:0007744|PDB:5F9C
ChainResidueDetails
BASP288
BASP290
BASP292
AASP288
AASP290
AASP292

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1
AMET1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS16
ALYS16

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
BTHR115
BTHR507
ATHR115
ATHR507

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:25288802, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
BSER117
ASER117

site_idSWS_FT_FI9
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P38652
ChainResidueDetails
BSER134
ASER477
ASER485
ASER541
BSER213
BSER369
BSER477
BSER485
BSER541
ASER134
ASER213
ASER369

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR185
ATHR185

site_idSWS_FT_FI11
Number of Residues10
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER201
ASER509
BSER206
BSER378
BSER505
BSER509
ASER201
ASER206
ASER378
ASER505

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
BLYS349
ALYS349

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
BTYR353
ATYR353

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D0F9
ChainResidueDetails
BLYS419
ALYS419

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PAK1 => ECO:0000269|PubMed:15378030
ChainResidueDetails
BTHR467
ATHR467

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PDB entries from 2024-06-19

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