eF-site ID 3zoo-D
PDB Code 3zoo
Chain D

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Title Structure of the Y46F mutant of human cytochrome c
Classification OXIDOREDUCTASE
Compound CYTOCHROME C
Source Homo sapiens (Human) (CYC_HUMAN)
Sequence D:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT
GQAPGFSYTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM
IFVGIKKKEERADLIAYLKKATNE
Description


Functional site

1) chain D
residue 55
type
sequence K
description BINDING SITE FOR RESIDUE HEC C 105
source : AC3

2) chain D
residue 13
type
sequence K
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

3) chain D
residue 14
type
sequence C
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

4) chain D
residue 17
type
sequence C
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

5) chain D
residue 18
type
sequence H
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

6) chain D
residue 28
type
sequence T
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

7) chain D
residue 30
type
sequence P
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

8) chain D
residue 40
type
sequence T
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

9) chain D
residue 41
type
sequence G
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

10) chain D
residue 48
type
sequence Y
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

11) chain D
residue 49
type
sequence T
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

12) chain D
residue 52
type
sequence N
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

13) chain D
residue 59
type
sequence W
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

14) chain D
residue 67
type
sequence Y
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

15) chain D
residue 78
type
sequence T
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

16) chain D
residue 79
type
sequence K
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

17) chain D
residue 80
type
sequence M
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

18) chain D
residue 81
type
sequence I
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

19) chain D
residue 82
type
sequence F
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

20) chain D
residue 85
type
sequence I
description BINDING SITE FOR RESIDUE HEC D 105
source : AC4

21) chain D
residue 79
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 1105
source : AC5

22) chain D
residue 14
type BINDING
sequence C
description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584
source Swiss-Prot : SWS_FT_FI1

23) chain D
residue 17
type BINDING
sequence C
description covalent => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584
source Swiss-Prot : SWS_FT_FI1

24) chain D
residue 18
type BINDING
sequence H
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:23150584
source Swiss-Prot : SWS_FT_FI2

25) chain D
residue 80
type BINDING
sequence M
description axial binding residue
source Swiss-Prot : SWS_FT_FI3

26) chain D
residue 1
type MOD_RES
sequence G
description N-acetylglycine => ECO:0000269|PubMed:13933734
source Swiss-Prot : SWS_FT_FI4

27) chain D
residue 48
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62894
source Swiss-Prot : SWS_FT_FI5

28) chain D
residue 97
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P62894
source Swiss-Prot : SWS_FT_FI5

29) chain D
residue 55
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P62897
source Swiss-Prot : SWS_FT_FI6

30) chain D
residue 72
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897
source Swiss-Prot : SWS_FT_FI7

31) chain D
residue 99
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P62897
source Swiss-Prot : SWS_FT_FI8


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