Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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_functionD-glucose 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
L0006749biological_processglutathione metabolic process
L0009051biological_processpentose-phosphate shunt, oxidative branch
L0009898cellular_componentcytoplasmic side of plasma membrane
L0010041biological_processresponse to iron(III) ion
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
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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P11411","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10745013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15858258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15858258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15858258","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BHL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"24769394","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

PDB statisticsPDBj update infoContact PDBjnumon