PDB: 1o94 Compound: trimethylamine dehydrogenase Classification: ELECTRON TRANSPORT Entry date in PDB: 2003-02-06 Resolution [Å]: 2.00 R-Factor: 0.174

CHAIN: A SWISS-PROT/TREMBL: P16099    KEYWORD: 3D-structure    4Fe-4S    Flavoprotein    FMN    Iron-sulfur    Oxidoreductase    EC: 1.5.8.2 SCOP: c.1.4.1 Alpha and beta proteins (a/b)    TIM beta/alpha-barrel    FMN-linked oxidoreductases    FMN-linked oxidoreductases    Trimethylamine dehydrogenase, N-terminal domain    Methylophilus methylotrophus, w3a1 SCOP: c.3.1.1 Alpha and beta proteins (a/b)    FAD/NAD(P)-binding domain    FAD/NAD(P)-binding domain    C-terminal domain of adrenodoxin reductase-like    Trimethylamine dehydrogenase, C-terminal domain    Methylophilus methylotrophus, w3a1 SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Trimethylamine dehydrogenase, middle domain    Methylophilus methylotrophus, w3a1 SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Trimethylamine dehydrogenase, middle domain    Methylophilus methylotrophus, w3a1 GO:  disulfide oxidoreductase activity    oxidoreductase activity    electron transport    CHAIN: B SWISS-PROT/TREMBL: P16099    KEYWORD: 3D-structure    4Fe-4S    Flavoprotein    FMN    Iron-sulfur    Oxidoreductase    EC: 1.5.8.2 SCOP: c.1.4.1 Alpha and beta proteins (a/b)    TIM beta/alpha-barrel    FMN-linked oxidoreductases    FMN-linked oxidoreductases    Trimethylamine dehydrogenase, N-terminal domain    Methylophilus methylotrophus, w3a1 SCOP: c.3.1.1 Alpha and beta proteins (a/b)    FAD/NAD(P)-binding domain    FAD/NAD(P)-binding domain    C-terminal domain of adrenodoxin reductase-like    Trimethylamine dehydrogenase, C-terminal domain    Methylophilus methylotrophus, w3a1 SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Trimethylamine dehydrogenase, middle domain    Methylophilus methylotrophus, w3a1 SCOP: c.4.1.1 Alpha and beta proteins (a/b)    Nucleotide-binding domain    Nucleotide-binding domain    N-terminal domain of adrenodoxin reductase-like    Trimethylamine dehydrogenase, middle domain    Methylophilus methylotrophus, w3a1 GO:  disulfide oxidoreductase activity    oxidoreductase activity    electron transport    CHAIN: C SWISS-PROT/TREMBL: P53570    KEYWORD: 3D-structure    Electron transport    FAD    Flavoprotein    SCOP: c.26.2.3 Alpha and beta proteins (a/b)    Adenine nucleotide alpha hydrolase-like    Adenine nucleotide alpha hydrolases-like    ETFP subunits    Small, beta subunit of electron transfer flavoprotein ETFP    Methylophilus methylotrophus GO:  electron transporter activity    electron transport    CHAIN: D SWISS-PROT/TREMBL: P53571    KEYWORD: 3D-structure    Electron transport    FAD    Flavoprotein    SCOP: c.26.2.3 Alpha and beta proteins (a/b)    Adenine nucleotide alpha hydrolase-like    Adenine nucleotide alpha hydrolases-like    ETFP subunits    Large, alpha subunit of electron transfer flavoprotein ETFP, N-terminal domain    Methylophilus methylotrophus GO:  electron transporter activity    electron transport    CHAIN: E SWISS-PROT/TREMBL: P53570    KEYWORD: 3D-structure    Electron transport    FAD    Flavoprotein    SCOP: c.26.2.3 Alpha and beta proteins (a/b)    Adenine nucleotide alpha hydrolase-like    Adenine nucleotide alpha hydrolases-like    ETFP subunits    Small, beta subunit of electron transfer flavoprotein ETFP    Methylophilus methylotrophus GO:  electron transporter activity    electron transport    CHAIN: F SWISS-PROT/TREMBL: P53571    KEYWORD: 3D-structure    Electron transport    FAD    Flavoprotein    SCOP: c.26.2.3 Alpha and beta proteins (a/b)    Adenine nucleotide alpha hydrolase-like    Adenine nucleotide alpha hydrolases-like    ETFP subunits    Large, alpha subunit of electron transfer flavoprotein ETFP, N-terminal domain    Methylophilus methylotrophus GO:  electron transporter activity    electron transport

Image Source: PDB

Loops in ArchDB40 clusters

1o94_A_13 - HA => SUBCLASS : 2.3.1
1o94_A_592 - HA => SUBCLASS : 2.6.1
1o94_A_137 - EH => SUBCLASS : 1.1.4
1o94_A_644 - EH => SUBCLASS : 1.1.28
1o94_A_75 - EH => SUBCLASS : 3.1.2
1o94_A_530 - EH => SUBCLASS : 3.7.2
1o94_A_75 - EH => SUBCLASS : 3.9.5
1o94_A_165 - EH => SUBCLASS : 3.31.1
1o94_A_530 - EH => SUBCLASS : 4.59.1
1o94_A_294 - EH => SUBCLASS : 5.43.1
1o94_A_631 - AR => SUBCLASS : 1.1.3
1o94_A_587 - AR => SUBCLASS : 1.2.2
1o94_A_637 - AR => SUBCLASS : 2.6.1
1o94_A_18 - AR => SUBCLASS : 3.8.2
1o94_A_18 - AR => SUBCLASS : 3.9.1
1o94_A_322 - HH => SUBCLASS : 1.2.7
1o94_A_566 - HH => SUBCLASS : 1.3.2

Loops in ArchDB95 clusters

1o94_A_318 - EH => SUBCLASS : 0.1.68
1o94_A_318 - EH => SUBCLASS : 0.1.76
1o94_A_644 - EH => SUBCLASS : 1.1.28
1o94_A_530 - EH => SUBCLASS : 2.1.37
1o94_A_137 - EH => SUBCLASS : 2.2.1
1o94_A_75 - EH => SUBCLASS : 3.2.1
1o94_A_165 - EH => SUBCLASS : 3.38.1
1o94_A_294 - EH => SUBCLASS : 5.58.1
1o94_A_587 - AR => SUBCLASS : 1.1.5
1o94_A_631 - AR => SUBCLASS : 1.2.1
1o94_A_637 - AR => SUBCLASS : 2.10.1
1o94_A_18 - AR => SUBCLASS : 3.4.1
1o94_A_322 - HH => SUBCLASS : 1.2.5
1o94_A_566 - HH => SUBCLASS : 1.3.2
1o94_A_566 - HH => SUBCLASS : 1.3.3
1o94_A_175 - HH => SUBCLASS : 14.10.1
1o94_C_194 - HE => SUBCLASS : 3.14.1
1o94_C_194 - HE => SUBCLASS : 3.14.2
1o94_A_13 - HA => SUBCLASS : 2.3.1
1o94_A_592 - HA => SUBCLASS : 2.4.1

Loops in ArchDB-EC clusters

1o94_A_566 - HH => SUBCLASS : 1.3.2

Loops not clustered in ArchDB

1o94_A_489 - AR
1o94_A_489 - AR
1o94_A_482 - AR
1o94_A_99 - AR
1o94_A_18 - AR
1o94_A_637 - AR
1o94_C_169 - AR
1o94_A_99 - AR
1o94_C_2 - AR
1o94_A_482 - AR
1o94_A_587 - AR
1o94_A_631 - AR
1o94_A_24 - EH
1o94_C_83 - EH
1o94_C_58 - EH
1o94_C_31 - EH
1o94_A_414 - EH
1o94_A_391 - EH
1o94_A_253 - EH
1o94_A_218 - EH
1o94_C_115 - EH
1o94_C_179 - EH
1o94_A_462 - EH
1o94_A_514 - EH
1o94_A_668 - EH
1o94_A_555 - EH
1o94_A_601 - HA
1o94_A_121 - HA
1o94_C_9 - HA
1o94_C_142 - HA
1o94_A_55 - HA
1o94_A_13 - HA
1o94_A_592 - HA
1o94_A_601 - HA
1o94_A_121 - HA
1o94_C_157 - HA
1o94_A_55 - HA
1o94_A_38 - HE
1o94_A_441 - HE
1o94_A_399 - HE
1o94_A_373 - HE
1o94_A_303 - HE
1o94_A_280 - HE
1o94_A_239 - HE
1o94_A_200 - HE
1o94_A_141 - HE
1o94_A_80 - HE
1o94_A_472 - HE
1o94_C_130 - HE
1o94_A_649 - HE
1o94_C_70 - HE
1o94_A_574 - HE
1o94_A_541 - HE
1o94_C_37 - HE
1o94_A_517 - HE
1o94_C_97 - HE
1o94_A_330 - HH
1o94_A_350 - HH
1o94_A_428 - HH
1o94_A_195 - HH

1djn A - percentage of sequence identity: 100
1djn B - percentage of sequence identity: 100
1djq A - percentage of sequence identity: 99
1djq B - percentage of sequence identity: 99
1o94 A - percentage of sequence identity: 100
1o94 B - percentage of sequence identity: 100
1o95 A - percentage of sequence identity: 100
1o95 B - percentage of sequence identity: 100
1o97 D - percentage of sequence identity: 100
2tmd A - percentage of sequence identity: 100
2tmd B - percentage of sequence identity: 100
null nu - percentage of sequence identity: 0