Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4GPZ

Crystal structure of human B type phosphoglycerate mutase H11 phosphorylated form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004082molecular_functionbisphosphoglycerate mutase activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0019901molecular_functionprotein kinase binding
A0034774cellular_componentsecretory granule lumen
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A1904813cellular_componentficolin-1-rich granule lumen
B0003824molecular_functioncatalytic activity
B0004082molecular_functionbisphosphoglycerate mutase activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0019901molecular_functionprotein kinase binding
B0034774cellular_componentsecretory granule lumen
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
ATRP68
AARG83
BTRP68
BARG83

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MES A 302
ChainResidue
AGLY24
AARG62
AGLU89
ATYR92
ALYS100
AHOH454
ANEP11
AASN17
AARG21
APHE22
ASER23

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 303
ChainResidue
AALA44
AASP47
AGLY234
AHOH514
AHOH533
AHOH585
BPRO125
BGLU127
BSER152

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsAwN
ChainResidueDetails
ALEU8-ASN17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:23653202, ECO:0000305|PubMed:15883004
ChainResidueDetails
ANEP11
BNEP11

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15883004
ChainResidueDetails
AGLU89
BGLU89

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15883004, ECO:0000269|PubMed:23653202
ChainResidueDetails
AARG10
ASER23
ALYS100
BARG10
BSER23
BLYS100

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q3JWH7
ChainResidueDetails
AARG62
AGLY187
BARG62
BGLY187

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15883004
ChainResidueDetails
AGLU89
AARG116
BGLU89
BARG116

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AHIS186
BHIS186

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER14
BSER14

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER23
BSER23

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:23653202
ChainResidueDetails
ATYR26
BTYR26

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER31
BSER31

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBJ1
ChainResidueDetails
ALYS106
BLYS106

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9DBJ1
ChainResidueDetails
ASER118
BSER118

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBJ1
ChainResidueDetails
ALYS251
BLYS251

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22157007
ChainResidueDetails
ALYS253
ALYS254
BLYS253
BLYS254

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon