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6VA9

Crystal structure of glucose-6-phosphate dehydrogenase R393H mutant in complex with catalytic NADP+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004345molecular_functionglucose-6-phosphate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005536molecular_functionglucose 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 Residues19
Detailsbinding site for residue NAP A 601
ChainResidue
ASER40
AALA127
ALEU142
APRO143
APRO144
ATYR147
AGLU170
ALYS171
APRO172
ATYR202
ATYR249
AGLY41
AASP42
ALEU43
AALA71
AARG72
ASER73
ATYR112
AASN126

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
AHIS393
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 Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7857286, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER8

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR10

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS89
ALYS432
ALYS497

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS171

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24769394, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS403

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR503

220113

PDB entries from 2024-05-22

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