eF-site ID 1y4g-C
PDB Code 1y4g
Chain C

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Title T-To-T(High) quaternary transitions in human hemoglobin: betaW37G deoxy low-salt (10 test sets)
Classification TRANSPORT PROTEIN
Compound Hemoglobin alpha chain
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence C:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK
TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKYR
Description


Functional site

1) chain C
residue 42
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

2) chain C
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

3) chain C
residue 45
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

4) chain C
residue 58
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

5) chain C
residue 61
type
sequence K
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

6) chain C
residue 83
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

7) chain C
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

8) chain C
residue 87
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

9) chain C
residue 91
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

10) chain C
residue 93
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

11) chain C
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

12) chain C
residue 98
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

13) chain C
residue 101
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

14) chain C
residue 136
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 142
source : AC3

15) chain C
residue 56
type
sequence K
description BINDING SITE FOR RESIDUE HEM D 147
source : AC4

16) chain C
residue 8
type CARBOHYD
sequence T
description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569
source Swiss-Prot : SWS_FT_FI12

17) chain C
residue 17
type CARBOHYD
sequence V
description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569
source Swiss-Prot : SWS_FT_FI12

18) chain C
residue 41
type CARBOHYD
sequence T
description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569
source Swiss-Prot : SWS_FT_FI12

19) chain C
residue 9
type BINDING
sequence N
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

20) chain C
residue 14
type BINDING
sequence W
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

21) chain C
residue 25
type BINDING
sequence G
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

22) chain C
residue 30
type BINDING
sequence E
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

23) chain C
residue 46
type BINDING
sequence F
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

24) chain C
residue 48
type BINDING
sequence L
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

25) chain C
residue 53
type BINDING
sequence A
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

26) chain C
residue 56
type BINDING
sequence K
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

27) chain C
residue 60
type BINDING
sequence K
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

28) chain C
residue 92
type BINDING
sequence R
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

29) chain C
residue 107
type BINDING
sequence V
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

30) chain C
residue 109
type BINDING
sequence L
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

31) chain C
residue 122
type BINDING
sequence H
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

32) chain C
residue 134
type BINDING
sequence T
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

33) chain C
residue 132
type MOD_RES
sequence V
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

34) chain C
residue 139
type MOD_RES
sequence K
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

35) chain C
residue 103
type MOD_RES
sequence H
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

36) chain C
residue 125
type MOD_RES
sequence L
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

37) chain C
residue 109
type MOD_RES
sequence L
description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
source Swiss-Prot : SWS_FT_FI11

38) chain C
residue 135
type MOD_RES
sequence V
description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
source Swiss-Prot : SWS_FT_FI11

39) chain C
residue 138
type MOD_RES
sequence S
description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
source Swiss-Prot : SWS_FT_FI11

40) chain C
residue 8
type MOD_RES
sequence T
description N-pyruvate 2-iminyl-valine; in Hb A1b
source Swiss-Prot : SWS_FT_FI6

41) chain C
residue 17
type MOD_RES
sequence V
description N-pyruvate 2-iminyl-valine; in Hb A1b
source Swiss-Prot : SWS_FT_FI6

42) chain C
residue 41
type MOD_RES
sequence T
description N-pyruvate 2-iminyl-valine; in Hb A1b
source Swiss-Prot : SWS_FT_FI6


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