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1FLG

CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA

Replaces:  1EEE
Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0006068biological_processethanol catabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0052934molecular_functionalcohol dehydrogenase (cytochrome c) activity
B0005509molecular_functioncalcium ion binding
B0006068biological_processethanol catabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
B0052934molecular_functionalcohol dehydrogenase (cytochrome c) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 751
ChainResidue
AGLU179
AASN266
AASP316
APQQ701

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 761
ChainResidue
AASP11
ATHR14
AASP17

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 752
ChainResidue
BASP316
BPQQ702
BGLU179
BASN266

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 762
ChainResidue
BASP11
BTHR14
BASP17

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PQQ A 701
ChainResidue
AGLU61
ACYS105
ACYS106
AARG111
ATHR155
ASER176
AGLY177
AASP178
ATRP248
AASN266
AARG344
AASN413
ATRP414
ATRP489
AGLY552
AALA553
ACA751

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PQQ B 702
ChainResidue
BGLU61
BCYS105
BCYS106
BARG111
BTHR155
BSER176
BGLY177
BASP178
BGLU179
BTRP248
BASN266
BARG344
BLEU409
BASN413
BTRP414
BTRP489
BGLY552
BALA553
BCA752

Functional Information from PROSITE/UniProt
site_idPS00363
Number of Residues29
DetailsBACTERIAL_PQQ_1 Bacterial quinoprotein dehydrogenases signature 1. DVlqyGMgthaqrWSplkqVNadNVfkLT
ChainResidueDetails
AASP17-THR45

site_idPS00364
Number of Residues22
DetailsBACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WqsasFDaetNTIIVgaGnpGP
ChainResidueDetails
ATRP248-PRO269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:10736230
ChainResidueDetails
AASP316
BASP316

site_idSWS_FT_FI2
Number of Residues26
DetailsBINDING: BINDING => ECO:0000269|PubMed:10736230, ECO:0007744|PDB:1FLG
ChainResidueDetails
AASP11
AASP316
AARG344
ATRP489
AALA553
BASP11
BTHR14
BASP17
BGLU61
BARG111
BTHR155
ATHR14
BHIS173
BGLU179
BASN266
BASP316
BARG344
BTRP489
BALA553
AASP17
AGLU61
AARG111
ATHR155
AHIS173
AGLU179
AASN266

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
AASP316

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
BASP316

222036

PDB entries from 2024-07-03

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