eF-site ID
|
6gcs-B |
PDB Code
|
6gcs |
Chain
|
B |
|
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Title
|
Cryo-EM structure of respiratory complex I from Yarrowia lipolytica |
Classification
|
OXIDOREDUCTASE |
Compound
|
75-KDA PROTEIN (NUAM) |
Source
|
ORGANISM_SCIENTIFIC: Yarrowia lipolytica; |
|
Sequence
|
B: |
GLKDQDRIFQNLYDNYGWDLASARKQGDWYKTKELILKGD
TWIIDEIKKSGLRGRGGAGFPSGLKWSFMNPPGWEKNEGP
RYLVVNADEGEPGTCKDREIMRKDPHKLVEGCLLAGRAMN
ATAAYIYIRGEFYNEAAVLQTAINEAYAAGLIGKDACGSG
YDFDVYIHRGMGAYVCGEETSLIESLEGKAGKPRLKPPFP
AGVGLFGRPSTVTNVETVAVAPTILRRGGDWFASFGRERN
SGTKLFCISGNVNEPCTVEEEMSIPLRELLEKHCGGIKGG
WDNLLGVIPGGCSVPILPKNICEDVLMDFDALKDVQSGLG
TAAVIVINKQQDVIRAIQRFAAFYKHESCGQCTPCREGTT
WLLKAMDRFRTGQAKEREIDMLYELTKDIEGHTICALGDA
AAWPIQGLIRNFRPEMETRMKKFHDEVGAVSVGGWMKDAR
VEK
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Description
|
(1) |
NUAM protein (E.C.1.6.99.3), NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (E.C.1.6.5.3,1.6.99.3), NUCM protein (E.C.1.6.99.3), NADH:ubiquinone reductase (H(+)-translocating), YALI0D24585p, YALI0E23089p, NUGM protein (E.C.1.6.99.3), Subunit NUHM of protein NADH:Ubiquinone Oxidoreductase (Complex I) (E.C.1.6.99.3), Subunit NUIM of protein NADH:Ubiquinone Oxidoreductase (Complex I) (E.C.1.6.99.3), YALI0E11891p, Subunit NUKM of protein NADH:Ubiquinone Oxidoreductase (Complex I) (E.C.1.6.99.3), NADH-ubiquinone oxidoreductase chain 4L (E.C.1.6.5.3), Acyl carrier protein, NADH-ubiquinone oxidoreductase, YALI0D10274p, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit N7BM, NUVM protein (E.C.1.6.99.3), NADH-ubiquinone oxidoreductase chain 1 (E.C.1.6.5.3), NADH-ubiquinone oxidoreductase chain 2 (E.C.1.6.5.3), NADH-ubiquinone oxidoreductase chain 3 (E.C.1.6.5.3), NADH-ubiquinone oxidoreductase chain 4 (E.C.1.6.5.3), NADH-ubiquinone oxidoreductase chain 5 (E.C.1.6.5.3), NADH-ubiquinone oxidoreductase chain 6 (E.C.1.6.5.3)
|
|
|
|
1)
|
chain |
B |
residue |
207 |
type |
|
sequence |
V
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
2)
|
chain |
B |
residue |
381 |
type |
|
sequence |
C
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
3)
|
chain |
B |
residue |
382 |
type |
|
sequence |
G
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
4)
|
chain |
B |
residue |
384 |
type |
|
sequence |
C
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
5)
|
chain |
B |
residue |
387 |
type |
|
sequence |
C
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
6)
|
chain |
B |
residue |
427 |
type |
|
sequence |
C
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
7)
|
chain |
B |
residue |
429 |
type |
|
sequence |
L
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
8)
|
chain |
B |
residue |
430 |
type |
|
sequence |
G
|
description |
binding site for residue SF4 B 501
|
source |
: AC4
|
|
9)
|
chain |
B |
residue |
86 |
type |
|
sequence |
G
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
10)
|
chain |
B |
residue |
87 |
type |
|
sequence |
R
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
11)
|
chain |
B |
residue |
88 |
type |
|
sequence |
G
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
12)
|
chain |
B |
residue |
97 |
type |
|
sequence |
K
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
13)
|
chain |
B |
residue |
118 |
type |
|
sequence |
N
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
14)
|
chain |
B |
residue |
120 |
type |
|
sequence |
D
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
15)
|
chain |
B |
residue |
121 |
type |
|
sequence |
E
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
16)
|
chain |
B |
residue |
122 |
type |
|
sequence |
G
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
17)
|
chain |
B |
residue |
206 |
type |
|
sequence |
Y
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
18)
|
chain |
B |
residue |
209 |
type |
|
sequence |
G
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
19)
|
chain |
B |
residue |
210 |
type |
|
sequence |
E
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
20)
|
chain |
B |
residue |
244 |
type |
|
sequence |
V
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
21)
|
chain |
B |
residue |
245 |
type |
|
sequence |
T
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
22)
|
chain |
B |
residue |
246 |
type |
|
sequence |
N
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
23)
|
chain |
B |
residue |
249 |
type |
|
sequence |
T
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
24)
|
chain |
B |
residue |
428 |
type |
|
sequence |
A
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
25)
|
chain |
B |
residue |
429 |
type |
|
sequence |
L
|
description |
binding site for residue FMN B 502
|
source |
: AC5
|
|
26)
|
chain |
B |
residue |
202-217 |
type |
prosite |
sequence |
GMGAYVCGEETSLIES
|
description |
COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GMGAYVCGEETSLIES
|
source |
prosite : PS00644
|
|
27)
|
chain |
B |
residue |
379-390 |
type |
prosite |
sequence |
ESCGQCTPCREG
|
description |
COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
|
source |
prosite : PS00645
|
|