eF-site ID 1qo8-A
PDB Code 1qo8
Chain A

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Title The structure of the open conformation of a flavocytochrome c3 fumarate reductase
Classification OXIDOREDUCTASE
Compound FLAVOCYTOCHROME C3 FUMARATE REDUCTASE
Source ORGANISM_SCIENTIFIC: SHEWANELLA FRIGIDIMARINA;
Sequence A:  TPDMGSFHADMGSCQSCHAKPIKVTDSETHENAQCKSCHG
EYAELANDKLQFDPHNSHLGDINCTSCHKGHEEPKFYCNE
CHSFDIKPMPFSDAKKKKSWDDGWDQDKIQKAIAAGPSET
TQVLVVGAGSAGFNASLAAKKAGANVILVDKAPFSGGNSM
ISAGGMNAVGTKQQTAHGVEDKVEWFIEDAMKGGRQQNDI
KLVTILAEQSADGVQWLESLGANLDDLKRSGGARVDRTHR
PHGGKSSGPEIIDTLRKAAKEQGIDTRLNSRVVKLVVNDD
HSVVGAVVHGKHTGYYMIGAKSVVLATGGYGMNKEMIAYY
RPTMKDMTSSNNITATGDGVLMAKEIGASMTDIDWVQAHP
TVGKDSRILISETVRGVGAVMVNKDGNRFISELTTRDKAS
DAILKQPGQFAWIIFDNQLYKKAKMVRGYDHLEMLYKGDT
VEQLAKSTGMKVADLAKTVSDYNGYVASGKDTAFGRADMP
LNMTQSPYYAVKVAPGIHHTMGGVAINTTASVLDLQSKPI
DGLFAAGEVTGGVHGYNRLGGNAIADTVVFGRIAGDNAAK
HALD
Description


Functional site
1) chain A
residue 53
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
2) chain A
residue 54
type
sequence D
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
3) chain A
residue 58
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
4) chain A
residue 59
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
5) chain A
residue 60
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
6) chain A
residue 79
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
7) chain A
residue 82
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
8) chain A
residue 83
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
9) chain A
residue 85
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
10) chain A
residue 162
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
11) chain A
residue 333
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
12) chain A
residue 369
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
13) chain A
residue 433
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 601
source : AC1
14) chain A
residue 40
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
15) chain A
residue 43
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
16) chain A
residue 46
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
17) chain A
residue 55
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
18) chain A
residue 56
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
19) chain A
residue 65
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
20) chain A
residue 68
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
21) chain A
residue 69
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
22) chain A
residue 88
type
sequence K
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
23) chain A
residue 90
type
sequence M
description BINDING SITE FOR RESIDUE HEM A 602
source : AC2
24) chain A
residue 5
type
sequence M
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
25) chain A
residue 9
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
26) chain A
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
27) chain A
residue 35
type
sequence Q
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
28) chain A
residue 36
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
29) chain A
residue 39
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
30) chain A
residue 40
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
31) chain A
residue 69
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
32) chain A
residue 91
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
33) chain A
residue 227
type
sequence D
description BINDING SITE FOR RESIDUE HEM A 603
source : AC3
34) chain A
residue 6
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
35) chain A
residue 9
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
36) chain A
residue 15
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
37) chain A
residue 18
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
38) chain A
residue 19
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
39) chain A
residue 29
type
sequence E
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
40) chain A
residue 66
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
41) chain A
residue 70
type
sequence K
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
42) chain A
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
43) chain A
residue 72
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
44) chain A
residue 293
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
45) chain A
residue 467
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
46) chain A
residue 468
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
47) chain A
residue 469
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
48) chain A
residue 470
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 604
source : AC4
49) chain A
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
50) chain A
residue 128
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
51) chain A
residue 130
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
52) chain A
residue 131
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
53) chain A
residue 132
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
54) chain A
residue 151
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
55) chain A
residue 152
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
56) chain A
residue 157
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
57) chain A
residue 158
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
58) chain A
residue 159
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
59) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
60) chain A
residue 163
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
61) chain A
residue 164
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
62) chain A
residue 165
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
63) chain A
residue 166
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
64) chain A
residue 271
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
65) chain A
residue 272
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
66) chain A
residue 273
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
67) chain A
residue 307
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
68) chain A
residue 308
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
69) chain A
residue 309
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
70) chain A
residue 331
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
71) chain A
residue 332
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
72) chain A
residue 335
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
73) chain A
residue 339
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
74) chain A
residue 499
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
75) chain A
residue 500
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
76) chain A
residue 528
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
77) chain A
residue 529
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
78) chain A
residue 539
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
79) chain A
residue 542
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
80) chain A
residue 543
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
81) chain A
residue 544
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
82) chain A
residue 545
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
83) chain A
residue 548
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 605
source : AC5
84) chain A
residue 397
type ACT_SITE
sequence R
description Proton donor => ECO:0000250|UniProtKB:P0C278
source Swiss-Prot : SWS_FT_FI1
85) chain A
residue 9
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
86) chain A
residue 19
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
87) chain A
residue 40
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
88) chain A
residue 56
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
89) chain A
residue 59
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
90) chain A
residue 69
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
91) chain A
residue 72
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
92) chain A
residue 83
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI2
93) chain A
residue 15
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
94) chain A
residue 18
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
95) chain A
residue 36
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
96) chain A
residue 39
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
97) chain A
residue 65
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
98) chain A
residue 68
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
99) chain A
residue 79
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
100) chain A
residue 82
type BINDING
sequence C
description covalent => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI3
101) chain A
residue 71
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
102) chain A
residue 165
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
103) chain A
residue 196
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
104) chain A
residue 360
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
105) chain A
residue 372
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
106) chain A
residue 373
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
107) chain A
residue 499
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
108) chain A
residue 539
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
109) chain A
residue 542
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P83223
source Swiss-Prot : SWS_FT_FI4
110) chain A
residue 132
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
111) chain A
residue 545
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
112) chain A
residue 151
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
113) chain A
residue 159
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
114) chain A
residue 160
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
115) chain A
residue 166
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
116) chain A
residue 273
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
117) chain A
residue 339
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
118) chain A
residue 529
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5
119) chain A
residue 544
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:10581549, ECO:0007744|PDB:1QO8
source Swiss-Prot : SWS_FT_FI5

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