eF-site ID 2a1u-AB
PDB Code 2a1u
Chain A, B

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Title Crystal structure of the human ETF E165betaA mutant
Classification ELECTRON TRANSPORT
Compound Electron transfer flavoprotein alpha-subunit, mitochondrial precursor
Source (ETFB_HUMAN)
Sequence A:  FQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGT
KCDKVAQDLCKVAGIAKVLVAQHDVYKGLLPEELTPLILA
TQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAI
KSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAAT
SGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVV
VSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVP
NDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVA
INKDPEAPIFQVADYGIVADLFKVVPEMTEILKKK
B:  LRVLVAVKRVIDYAVKIRVKPDRTGVVTDGVKHSMNPFCE
IAVEEAVRLKEKKLVKEVIAVSCGPAQCQETIRTALAMGA
DRGIHVEVPPAEAERLGPLQVARVLAKLAEKEKVDLVLLG
KQAIDDDCNQTGQMTAGFLDWPQGTFASQVTLEGDKLKVE
RAIDGGLETLRLKLPAVVTADLRLNEPRYATLPNIMKAKK
KKIEVIKPGDLGVDLTSKLSVISVEDPPQRTAGVKVETTE
DLVAKLKEIGRI
Description


Functional site
1) chain A
residue 208
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
2) chain A
residue 222
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
3) chain A
residue 223
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
4) chain A
residue 224
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
5) chain A
residue 248
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
6) chain A
residue 249
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
7) chain A
residue 250
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
8) chain A
residue 262
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
9) chain A
residue 263
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
10) chain A
residue 264
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
11) chain A
residue 265
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
12) chain A
residue 266
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
13) chain A
residue 267
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
14) chain A
residue 279
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
15) chain A
residue 280
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
16) chain A
residue 281
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
17) chain A
residue 285
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
18) chain A
residue 286
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
19) chain A
residue 300
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
20) chain A
residue 301
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
21) chain A
residue 302
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
22) chain A
residue 317
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
23) chain A
residue 318
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
24) chain A
residue 319
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
25) chain B
residue 185
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 599
source : AC1
26) chain B
residue 9
type
sequence A
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
27) chain B
residue 10
type
sequence V
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
28) chain B
residue 11
type
sequence K
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
29) chain B
residue 39
type
sequence N
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
30) chain B
residue 42
type
sequence C
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
31) chain B
residue 66
type
sequence C
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
32) chain B
residue 104
type
sequence V
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
33) chain B
residue 122
type
sequence L
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
34) chain B
residue 123
type
sequence G
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
35) chain B
residue 125
type
sequence Q
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
36) chain B
residue 126
type
sequence A
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
37) chain B
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
38) chain B
residue 131
type
sequence C
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
39) chain B
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
40) chain B
residue 133
type
sequence Q
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
41) chain B
residue 134
type
sequence T
description BINDING SITE FOR RESIDUE AMP B 600
source : AC2
42) chain A
residue 274-300
type prosite
sequence LYIAVGISGAIQHLAGMKDSKTIVAIN
description ETF_ALPHA Electron transfer flavoprotein alpha-subunit signature. LYIAvGISGaIQHlaGmkdsktIvAIN
source prosite : PS00696
43) chain B
residue 162-182
type prosite
sequence VERAIDGGLETLRLKLPAVVT
description ETF_BETA Electron transfer flavoprotein beta-subunit signature. VeRaiDGGl.EtLrlklPaVVT
source prosite : PS01065
44) chain B
residue 9
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
source Swiss-Prot : SWS_FT_FI1
45) chain B
residue 39
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
source Swiss-Prot : SWS_FT_FI1
46) chain B
residue 66
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
source Swiss-Prot : SWS_FT_FI1
47) chain B
residue 123
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
source Swiss-Prot : SWS_FT_FI1
48) chain A
residue 300
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
source Swiss-Prot : SWS_FT_FI1
49) chain A
residue 318
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055, ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T
source Swiss-Prot : SWS_FT_FI1
50) chain A
residue 69
type MOD_RES
sequence K
description N-acetylalanine => ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
51) chain A
residue 85
type MOD_RES
sequence K
description N-acetylalanine => ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
52) chain A
residue 158
type MOD_RES
sequence K
description N-acetylalanine => ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
53) chain A
residue 203
type MOD_RES
sequence K
description N-acetylalanine => ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
54) chain A
residue 226
type MOD_RES
sequence K
description N-acetylalanine => ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
55) chain A
residue 232
type MOD_RES
sequence K
description N-acetylalanine => ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI2
56) chain B
residue 200
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI3
57) chain A
residue 75
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI3
58) chain A
residue 101
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI3
59) chain A
residue 139
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI3
60) chain A
residue 164
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI3
61) chain B
residue 203
type MOD_RES
sequence K
description N6,N6,N6-trimethyllysine; by ETFBKMT => ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:25416781
source Swiss-Prot : SWS_FT_FI4
62) chain B
residue 210
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCW4
source Swiss-Prot : SWS_FT_FI5
63) chain B
residue 248
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCW4
source Swiss-Prot : SWS_FT_FI5
64) chain B
residue 223
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6
65) chain B
residue 226
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6
66) chain A
residue 301
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6
67) chain B
residue 238
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCW4
source Swiss-Prot : SWS_FT_FI7

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