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4LGV

X-ray crystal structure of Glucose-6-phosphate 1-dehydrogenase from Mycobacterium avium

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
B0004345molecular_functionglucose-6-phosphate dehydrogenase activity
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006098biological_processpentose-phosphate shunt
B0009051biological_processpentose-phosphate shunt, oxidative branch
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0050661molecular_functionNADP binding
C0004345molecular_functionglucose-6-phosphate dehydrogenase activity
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0006098biological_processpentose-phosphate shunt
C0009051biological_processpentose-phosphate shunt, oxidative branch
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0050661molecular_functionNADP binding
D0004345molecular_functionglucose-6-phosphate dehydrogenase activity
D0005829cellular_componentcytosol
D0006006biological_processglucose metabolic process
D0006098biological_processpentose-phosphate shunt
D0009051biological_processpentose-phosphate shunt, oxidative branch
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AARG61
AASP73
AASP77
BASP50
CPRO286

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AARG32
AGLU390
AARG393

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AASP20
AGLY19

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BARG432
BHIS434
DASN344
DHOH650
DHOH680

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 501
ChainResidue
CLEU39
CGLU40
CHIS41
CPHE403

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL C 502
ChainResidue
CHIS335

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 503
ChainResidue
CARG317
CGLN457

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL D 501
ChainResidue
DHIS335

Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHFLGKQ
ChainResidueDetails
AASP171-GLN177

249697

PDB entries from 2026-02-25

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