eF-site ID 1ege-B
PDB Code 1ege
Chain B

click to enlarge
Title STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE
Classification ELECTRON TRANSFER
Compound MEDIUM CHAIN ACYL-COA DEHYDROGENASE
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence B:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP
VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY
GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL
MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN
GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG
RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM
GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV
EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA
SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA
KIYQIYEGTSQIQRLIVAREHIDKYKN
Description


Functional site

1) chain B
residue 376
type
sequence E
description CATALYTIC BASE IN CHAIN B
source : CA2

2) chain B
residue 281
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

3) chain B
residue 283
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

4) chain B
residue 284
type
sequence F
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

5) chain B
residue 288
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

6) chain B
residue 291
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

7) chain B
residue 294
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

8) chain B
residue 349
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

9) chain B
residue 350
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

10) chain B
residue 352
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

11) chain B
residue 353
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 399
source : AC1

12) chain B
residue 133
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

13) chain B
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

14) chain B
residue 136
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

15) chain B
residue 141
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

16) chain B
residue 142
type
sequence S
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

17) chain B
residue 166
type
sequence W
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

18) chain B
residue 167
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

19) chain B
residue 168
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

20) chain B
residue 214
type
sequence N
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

21) chain B
residue 371
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

22) chain B
residue 375
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

23) chain B
residue 376
type
sequence E
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

24) chain B
residue 378
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

25) chain B
residue 380
type
sequence Q
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2

26) chain B
residue 292
type
sequence Q
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3

27) chain B
residue 376
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 133
type BINDING
sequence Y
description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 166
type BINDING
sequence W
description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 291
type BINDING
sequence H
description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 142
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3

32) chain B
residue 253
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 256
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3

34) chain B
residue 376
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3

35) chain B
residue 281
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
source Swiss-Prot : SWS_FT_FI4

36) chain B
residue 349
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13
source Swiss-Prot : SWS_FT_FI4

37) chain B
residue 246
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5

38) chain B
residue 44
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5

39) chain B
residue 187
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5

40) chain B
residue 192
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5

41) chain B
residue 234
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5

42) chain B
residue 154
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI6

43) chain B
residue 254
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

44) chain B
residue 276
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

45) chain B
residue 326
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI8


Display surface

Download
Links