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

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 C:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP
VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY
GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL
MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN
GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG
RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM
GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV
EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA
SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA
KIYQIYEGTSQIQRLIVAREHIDKYKN
Description


Functional site
1) chain C
residue 376
type
sequence E
description CATALYTIC BASE IN CHAIN C
source : CA3
2) chain C
residue 292
type
sequence Q
description BINDING SITE FOR RESIDUE FAD B 399
source : AC2
3) chain C
residue 133
type
sequence Y
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
4) chain C
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
5) chain C
residue 136
type
sequence T
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
6) chain C
residue 141
type
sequence G
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
7) chain C
residue 142
type
sequence S
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
8) chain C
residue 166
type
sequence W
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
9) chain C
residue 168
type
sequence T
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
10) chain C
residue 222
type
sequence T
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
11) chain C
residue 371
type
sequence I
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
12) chain C
residue 374
type
sequence I
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
13) chain C
residue 375
type
sequence Y
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
14) chain C
residue 376
type
sequence E
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
15) chain C
residue 378
type
sequence T
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
16) chain C
residue 380
type
sequence Q
description BINDING SITE FOR RESIDUE FAD C 399
source : AC3
17) chain C
residue 281
type
sequence R
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
18) chain C
residue 283
type
sequence T
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
19) chain C
residue 284
type
sequence F
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
20) chain C
residue 288
type
sequence L
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
21) chain C
residue 291
type
sequence H
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
22) chain C
residue 294
type
sequence I
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
23) chain C
residue 349
type
sequence Q
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
24) chain C
residue 350
type
sequence I
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
25) chain C
residue 352
type
sequence G
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
26) chain C
residue 353
type
sequence G
description BINDING SITE FOR RESIDUE FAD D 399
source : AC4
27) chain C
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 C
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 C
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 C
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 C
residue 253
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3
32) chain C
residue 256
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3
33) chain C
residue 376
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3
34) chain C
residue 142
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC
source Swiss-Prot : SWS_FT_FI3
35) chain C
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 C
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 C
residue 44
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5
38) chain C
residue 187
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5
39) chain C
residue 192
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5
40) chain C
residue 234
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5
41) chain C
residue 246
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI5
42) chain C
residue 154
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI6
43) chain C
residue 254
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7
44) chain C
residue 276
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7
45) chain C
residue 326
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P45952
source Swiss-Prot : SWS_FT_FI8

Display surface

Download
Links