eF-site ID 2n3y_15-A
PDB Code 2n3y
Model 15
Chain A

click to enlarge
Title NMR structure of the Y48pCMF variant of human cytochrome c in its reduced state
Classification ELECTRON TRANSPORT
Compound Cytochrome c
Source Homo sapiens (Human) (CYC_HUMAN)
Sequence A:  GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKT
GQAPGYSXTAANKNKGIIWGEDTLMEYLENPKKYIPGTKM
IFVGIKKKEERADLIAYLKKATNE
Description (1)  Cytochrome c


Functional site

1) chain A
residue 13
type
sequence K
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

2) chain A
residue 14
type
sequence C
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

3) chain A
residue 17
type
sequence C
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

4) chain A
residue 18
type
sequence H
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

5) chain A
residue 28
type
sequence T
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

6) chain A
residue 30
type
sequence P
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

7) chain A
residue 40
type
sequence T
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

8) chain A
residue 47
type
sequence S
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

9) chain A
residue 48
type
sequence X
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

10) chain A
residue 49
type
sequence T
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

11) chain A
residue 67
type
sequence Y
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

12) chain A
residue 79
type
sequence K
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

13) chain A
residue 80
type
sequence M
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

14) chain A
residue 85
type
sequence I
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

15) chain A
residue 94
type
sequence L
description BINDING SITE FOR RESIDUE MH0 A 201
source : AC1

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

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

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

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

20) chain A
residue 48
type MOD_RES
sequence X
description Phosphotyrosine => ECO:0000250|UniProtKB:P62894
source Swiss-Prot : SWS_FT_FI5

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

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


Display surface

Download
Links