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6E08

Crystal structure of G6PD in complex with structural NADP

Replaces:  5VFL
Functional Information from GO Data
ChainGOidnamespacecontents
L0004345molecular_functionglucose-6-phosphate dehydrogenase activity
L0005515molecular_functionprotein binding
L0005536molecular_functionglucose binding
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0006006biological_processglucose metabolic process
L0006098biological_processpentose-phosphate shunt
L0006629biological_processlipid metabolic process
L0006695biological_processcholesterol biosynthetic process
L0006739biological_processNADP metabolic process
L0006740biological_processNADPH regeneration
L0006749biological_processglutathione metabolic process
L0009051biological_processpentose-phosphate shunt, oxidative branch
L0009898cellular_componentcytoplasmic side of plasma membrane
L0010041biological_processresponse to iron(III) ion
L0010734biological_processnegative regulation of protein glutathionylation
L0014070biological_processresponse to organic cyclic compound
L0016020cellular_componentmembrane
L0016491molecular_functionoxidoreductase activity
L0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
L0019322biological_processpentose biosynthetic process
L0021762biological_processsubstantia nigra development
L0030246molecular_functioncarbohydrate binding
L0032094biological_processresponse to food
L0034451cellular_componentcentriolar satellite
L0034599biological_processcellular response to oxidative stress
L0042802molecular_functionidentical protein binding
L0042803molecular_functionprotein homodimerization activity
L0043231cellular_componentintracellular membrane-bounded organelle
L0043249biological_processerythrocyte maturation
L0043523biological_processregulation of neuron apoptotic process
L0045471biological_processresponse to ethanol
L0046390biological_processribose phosphate biosynthetic process
L0050661molecular_functionNADP binding
L0051156biological_processglucose 6-phosphate metabolic process
L0061052biological_processnegative regulation of cell growth involved in cardiac muscle cell development
L0070062cellular_componentextracellular exosome
L1904879biological_processpositive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel
L2000378biological_processnegative regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue NAP L 601
ChainResidue
LLYS238
LASP493
LMET496
LPHE501
LTYR503
LTYR507
LTRP509
LHOH710
LHOH716
LHOH725
LHOH736
LLYS366
LHOH756
LHOH759
LHOH766
LHOH793
LHOH831
LHOH835
LARG370
LARG393
LTYR401
LLYS403
LASP421
LTHR423
LARG487

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL L 602
ChainResidue
LARG219
LARG227
LASP350
LASP375
LHOH825
LHOH980

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL L 603
ChainResidue
LLYS293
LCYS294
LILE295
LGLU345
LARG463
LHOH749
LHOH938

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL L 604
ChainResidue
LLYS171
LHIS201
LPHE237
LGLU239
LASP258
LVAL259
LHIS263

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL L 605
ChainResidue
LTYR343
LHOH727

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL L 606
ChainResidue
LLYS497
LARG498

Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE
ChainResidueDetails
LASP200-GLU206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P11411
ChainResidueDetails
LHIS263

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
LGLY38
LARG487
LTYR503
LTRP509
LARG72
LTYR147
LARG357
LLYS366
LARG370
LARG393
LTYR401
LASP421

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15858258, ECO:0007744|PDB:2BH9
ChainResidueDetails
LLYS171
LHIS201
LGLU239
LASP258

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15858258, ECO:0007744|PDB:2BHL
ChainResidueDetails
LLYS360
LARG365
LGLN395

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
LALA2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
LSER8

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
LTHR10

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
LLYS89
LLYS432
LLYS497

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
LLYS171

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24769394, ECO:0007744|PubMed:19608861
ChainResidueDetails
LLYS403

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
LTYR503

218853

PDB entries from 2024-04-24

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