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

2DPG

COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004345molecular_functionglucose-6-phosphate dehydrogenase activity
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006098biological_processpentose-phosphate shunt
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE NAP A 799
ChainResidue
AGLY12
AASP85
AVAL86
AVAL118
ATHR14
AGLY15
AASP16
ALEU17
AALA45
AARG46
AGLN47
AHIS84

Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE
ChainResidueDetails
AASP177-GLU183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:9485426
ChainResidueDetails
ATHR241

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304, ECO:0000269|PubMed:9485426
ChainResidueDetails
AGLY13
AGLN47
AVAL86

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11320304
ChainResidueDetails
APRO149

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106478
ChainResidueDetails
ATYR179
AGLU183
AVAL217
AMET236
AARG339
AGLN344

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dpg
ChainResidueDetails
AASP177
AASN240

site_idMCSA1
Number of Residues3
DetailsM-CSA 843
ChainResidueDetails
AASP177modifies pKa
AHIS178transition state stabiliser
AASN240proton acceptor, proton donor

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon