eF-site ID 1umd-C
PDB Code 1umd
Chain C

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Title branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methyl-2-oxopentanoate as an intermediate
Classification OXIDOREDUCTASE
Compound 2-oxo acid dehydrogenase alpha subunit
Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (ODBB_THET8)
Sequence C:  HRFETFTEEPIRLIGEEGEWLGDFPLDLEGEKLRRLYRDM
LAARMLDERYTILIRTGKTSFIAPAAGHEAAQVAIAHAIR
PGFDWVFPYYRDHGLALALGIPLKELLGQMLATKADPNKG
RQMPEHPGSKALNFFTVASPIASHVPPAAGAAISMKLLRT
GQVAVCTFGDGATSEGDWYAGINFAAVQGAPAVFIAENNF
YAISVDYRHQTHSPTIADKAHAFGIPGYLVDGMDVLASYY
VVKEAVERARRGEGPSLVELRVYRYGPHSSADDDSRYRPK
EEVAFWRKKDPIPRFRRFLEARGLWNEEWEEDVREEIRAE
LERGLKEAEEAGPVPPEWMFEDVFAEKPWHLLRQEALLKE
E
Description


Functional site

1) chain C
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE MG C 2401
source : AC2

2) chain C
residue 204
type
sequence N
description BINDING SITE FOR RESIDUE MG C 2401
source : AC2

3) chain C
residue 206
type
sequence Y
description BINDING SITE FOR RESIDUE MG C 2401
source : AC2

4) chain C
residue 94
type
sequence Y
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

5) chain C
residue 95
type
sequence Y
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

6) chain C
residue 96
type
sequence R
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

7) chain C
residue 144
type
sequence S
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

8) chain C
residue 145
type
sequence P
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

9) chain C
residue 146
type
sequence I
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

10) chain C
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

11) chain C
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

12) chain C
residue 176
type
sequence G
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

13) chain C
residue 177
type
sequence A
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

14) chain C
residue 180
type
sequence E
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

15) chain C
residue 204
type
sequence N
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

16) chain C
residue 206
type
sequence Y
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

17) chain C
residue 207
type
sequence A
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

18) chain C
residue 208
type
sequence I
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

19) chain C
residue 273
type
sequence H
description BINDING SITE FOR RESIDUE TPP C 2402
source : AC5

20) chain C
residue 66
type
sequence F
description BINDING SITE FOR RESIDUE COI C 2403
source : AC6

21) chain C
residue 144
type
sequence S
description BINDING SITE FOR RESIDUE COI C 2403
source : AC6

22) chain C
residue 66
type ACT_SITE
sequence F
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

23) chain C
residue 94
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

24) chain C
residue 95
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

25) chain C
residue 128
type ACT_SITE
sequence M
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

26) chain C
residue 144
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 174
type ACT_SITE
sequence G
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

28) chain C
residue 175
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

29) chain C
residue 204
type ACT_SITE
sequence N
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

30) chain C
residue 206
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

31) chain C
residue 273
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1


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