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

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Title THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION
Classification ELECTRON TRANSPORT
Compound FERROCYTOCHROME C
Source null (CYC_KATPE)
Sequence B:  GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKT
GQAEGYSYTDANKSKGIVWNENTLMEYLENPKKYIPGTKM
IFAGIKKKGERQDLVAYLKSATS
Description (1)  FERROCYTOCHROME C


Functional site

1) chain B
residue 13
type
sequence K
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

2) chain B
residue 14
type
sequence C
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

3) chain B
residue 17
type
sequence C
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

4) chain B
residue 18
type
sequence H
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

5) chain B
residue 32
type
sequence L
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

6) chain B
residue 35
type
sequence L
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

7) chain B
residue 38
type
sequence R
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

8) chain B
residue 40
type
sequence T
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

9) chain B
residue 46
type
sequence Y
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

10) chain B
residue 48
type
sequence Y
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

11) chain B
residue 52
type
sequence N
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

12) chain B
residue 59
type
sequence W
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

13) chain B
residue 78
type
sequence T
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

14) chain B
residue 79
type
sequence K
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

15) chain B
residue 80
type
sequence M
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

16) chain B
residue 82
type
sequence F
description BINDING SITE FOR RESIDUE HEC B 104
source : AC2

17) chain B
residue 15
type BINDING
sequence A
description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 18
type BINDING
sequence H
description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 19
type BINDING
sequence T
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 81
type BINDING
sequence I
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:166072
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 2
type MOD_RES
sequence D
description N-acetylglycine => ECO:0000269|PubMed:5106585
source Swiss-Prot : SWS_FT_FI3


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