eF-site ID 2wp9-B
PDB Code 2wp9
Chain B

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Title Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhB His207Thr mutant
Classification OXIDOREDUCTASE
Compound SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
Source (DHSD_ECOLI)
Sequence B:  MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALI
QLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPIS
ALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPY
LLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCP
SFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDA
FSVFRCTSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA
Description


Functional site

1) chain B
residue 54
type
sequence S
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

2) chain B
residue 55
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

3) chain B
residue 56
type
sequence R
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

4) chain B
residue 58
type
sequence G
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

5) chain B
residue 59
type
sequence V
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

6) chain B
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

7) chain B
residue 61
type
sequence G
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

8) chain B
residue 63
type
sequence D
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

9) chain B
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC4

10) chain B
residue 149
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

11) chain B
residue 150
type
sequence I
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

12) chain B
residue 152
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

13) chain B
residue 153
type
sequence A
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

14) chain B
residue 155
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

15) chain B
residue 216
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

16) chain B
residue 217
type
sequence P
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC5

17) chain B
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

18) chain B
residue 206
type
sequence C
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

19) chain B
residue 207
type
sequence T
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

20) chain B
residue 208
type
sequence S
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

21) chain B
residue 210
type
sequence M
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

22) chain B
residue 211
type
sequence N
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

23) chain B
residue 212
type
sequence C
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

24) chain B
residue 223
type
sequence T
description BINDING SITE FOR RESIDUE F3S B 304
source : AC6

25) chain B
residue 207
type
sequence T
description BINDING SITE FOR RESIDUE HEM C 1129
source : AC7

26) chain B
residue 160
type
sequence P
description BINDING SITE FOR RESIDUE CBE C 1130
source : AC8

27) chain B
residue 161
type
sequence S
description BINDING SITE FOR RESIDUE CBE C 1130
source : AC8

28) chain B
residue 164
type
sequence W
description BINDING SITE FOR RESIDUE CBE C 1130
source : AC8

29) chain B
residue 207
type
sequence T
description BINDING SITE FOR RESIDUE CBE C 1130
source : AC8

30) chain B
residue 149-160
type prosite
sequence CILCACCSTSCP
description 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
source prosite : PS00198

31) chain B
residue 216
type TOPO_DOM
sequence C
description Cytoplasmic => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 159
type TOPO_DOM
sequence C
description Cytoplasmic => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 206
type TOPO_DOM
sequence C
description Cytoplasmic => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 212
type TOPO_DOM
sequence C
description Cytoplasmic => ECO:0000305
source Swiss-Prot : SWS_FT_FI1


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