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6JYU

Crystal structure of Human G6PD Canton

Functional Information from GO Data
ChainGOidnamespacecontents
A0004345molecular_functionglucose-6-phosphate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005536molecular_functionD-glucose binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006098biological_processpentose-phosphate shunt
A0006629biological_processlipid metabolic process
A0006695biological_processcholesterol biosynthetic process
A0006739biological_processNADP metabolic process
A0006740biological_processNADPH regeneration
A0006749biological_processglutathione metabolic process
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010041biological_processresponse to iron(III) ion
A0010734biological_processnegative regulation of protein glutathionylation
A0014070biological_processresponse to organic cyclic compound
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0019322biological_processpentose biosynthetic process
A0021762biological_processsubstantia nigra development
A0030246molecular_functioncarbohydrate binding
A0032094biological_processresponse to food
A0034451cellular_componentcentriolar satellite
A0034599biological_processcellular response to oxidative stress
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0043249biological_processerythrocyte maturation
A0043523biological_processregulation of neuron apoptotic process
A0045471biological_processresponse to ethanol
A0046390biological_processribose phosphate biosynthetic process
A0050661molecular_functionNADP binding
A0051156biological_processglucose 6-phosphate metabolic process
A0061052biological_processnegative regulation of cell growth involved in cardiac muscle cell development
A0070062cellular_componentextracellular exosome
A1904879biological_processpositive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
A2000378biological_processnegative regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue NAP A 601
ChainResidue
ALYS238
ATHR423
AARG487
AASP493
APHE501
ATYR503
ATYR507
ATRP509
AHOH705
AHOH710
AHOH711
AGLU364
AHOH716
AHOH742
AHOH771
AHOH796
AHOH843
AHOH857
AHOH1043
AHOH1115
ALYS366
AARG370
AARG393
AASN397
ATYR401
ALYS403
AASP421

Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE
ChainResidueDetails
AASP200-GLU206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P11411
ChainResidueDetails
AHIS263

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:10745013, ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI, ECO:0007744|PDB:2BH9
ChainResidueDetails
AGLY38
AARG487
ATYR503
ATRP509
AARG72
ATYR147
AARG357
ALYS366
AARG370
AARG393
ATYR401
AASP421

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15858258, ECO:0007744|PDB:2BH9
ChainResidueDetails
ALYS171
AHIS201
AGLU239
AASP258

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15858258, ECO:0007744|PDB:2BHL
ChainResidueDetails
ALYS360
AARG365
AGLN395

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS89
ALYS432
ALYS497

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS171

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24769394, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS403

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR503

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PDB entries from 2024-07-17

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