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

3B4Y

FGD1 (Rv0407) from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0045454biological_processcell redox homeostasis
A0052749molecular_functionglucose-6-phosphate dehydrogenase (coenzyme F420) activity
A0070967molecular_functioncoenzyme F420 binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0045454biological_processcell redox homeostasis
B0052749molecular_functionglucose-6-phosphate dehydrogenase (coenzyme F420) activity
B0070967molecular_functioncoenzyme F420 binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE F42 A 338
ChainResidue
ASER38
AGLU109
AASN112
APHE125
AALA175
AALA176
AGLY177
AGLY178
APRO179
AALA180
AVAL181
AASP39
ATHR195
AGLU230
AHIS260
AFLC337
AHOH339
AHOH341
AHOH368
AHOH402
AHIS40
ASER73
AVAL74
ATHR76
AGLY106
ATHR107
AGLY108

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FLC A 337
ChainResidue
ATRP44
AGLU109
ATHR195
ALYS198
ALYS232
ALEU252
ALYS259
AHIS260
AARG283
AF42338
AHOH368
AHOH411
AHOH424

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE F42 B 338
ChainResidue
BSER38
BASP39
BHIS40
BSER73
BVAL74
BTHR76
BGLY106
BTHR107
BGLY108
BGLU109
BASN112
BPHE125
BALA175
BALA176
BGLY177
BGLY178
BPRO179
BALA180
BVAL181
BTHR195
BGLU230
BHIS260
BFLC337
BHOH345
BHOH351
BHOH355
BHOH358
BHOH360
BHOH425

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FLC B 337
ChainResidue
BTRP44
BGLU109
BTHR195
BLYS198
BLYS232
BLEU252
BLYS259
BHIS260
BARG283
BF42338
BHOH346
BHOH358
BHOH403

Functional Information from PROSITE/UniProt
site_idPS00683
Number of Residues11
DetailsRHODANESE_2 Rhodanese C-terminal signature. AtgYEGAWpEF
ChainResidueDetails
AALA115-PHE125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:18434308
ChainResidueDetails
AHIS40
BHIS40

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:18434308
ChainResidueDetails
AGLU109
BGLU109

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:18434308, ECO:0007744|PDB:3B4Y
ChainResidueDetails
AASP39
ATHR107
AASN112
AGLY177
BASP39
BTHR107
BASN112
BGLY177

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:18434308
ChainResidueDetails
ATHR76
BLYS198
BLYS259
BARG283
AALA180
ATHR195
ALYS198
ALYS259
AARG283
BTHR76
BALA180
BTHR195

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rhc
ChainResidueDetails
AGLU109
ATRP44
AHIS40

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rhc
ChainResidueDetails
BGLU109
BTRP44
BHIS40

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon