eF-site ID 5ksi-C
PDB Code 5ksi
Chain C

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Title Crystal structure of deoxygenated hemoglobin in complex with sphingosine phosphate and 2,3-Bisphosphoglycerate
Classification OXYGEN TRANSPORT
Compound Hemoglobin subunit alpha
Source ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence C:  VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTK
TYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKYR
Description


Functional site

1) chain C
residue 32
type
sequence M
description binding site for residue HEM C 201
source : AC6

2) chain C
residue 42
type
sequence Y
description binding site for residue HEM C 201
source : AC6

3) chain C
residue 43
type
sequence F
description binding site for residue HEM C 201
source : AC6

4) chain C
residue 45
type
sequence H
description binding site for residue HEM C 201
source : AC6

5) chain C
residue 46
type
sequence F
description binding site for residue HEM C 201
source : AC6

6) chain C
residue 58
type
sequence H
description binding site for residue HEM C 201
source : AC6

7) chain C
residue 61
type
sequence K
description binding site for residue HEM C 201
source : AC6

8) chain C
residue 83
type
sequence L
description binding site for residue HEM C 201
source : AC6

9) chain C
residue 86
type
sequence L
description binding site for residue HEM C 201
source : AC6

10) chain C
residue 87
type
sequence H
description binding site for residue HEM C 201
source : AC6

11) chain C
residue 91
type
sequence L
description binding site for residue HEM C 201
source : AC6

12) chain C
residue 93
type
sequence V
description binding site for residue HEM C 201
source : AC6

13) chain C
residue 97
type
sequence N
description binding site for residue HEM C 201
source : AC6

14) chain C
residue 98
type
sequence F
description binding site for residue HEM C 201
source : AC6

15) chain C
residue 101
type
sequence L
description binding site for residue HEM C 201
source : AC6

16) chain C
residue 136
type
sequence L
description binding site for residue HEM C 201
source : AC6

17) chain C
residue 36
type
sequence F
description binding site for residue S1P C 202
source : AC7

18) chain C
residue 99
type
sequence K
description binding site for residue S1P C 202
source : AC7

19) chain C
residue 100
type
sequence L
description binding site for residue S1P C 202
source : AC7

20) chain C
residue 103
type
sequence H
description binding site for residue S1P C 202
source : AC7

21) chain C
residue 41
type
sequence T
description binding site for residue S1P C 203
source : AC8

22) chain C
residue 42
type
sequence Y
description binding site for residue S1P C 203
source : AC8

23) chain C
residue 44
type
sequence P
description binding site for residue S1P C 203
source : AC8

24) chain C
residue 90
type
sequence K
description binding site for residue S1P C 203
source : AC8

25) chain C
residue 91
type
sequence L
description binding site for residue S1P C 203
source : AC8

26) chain C
residue 92
type
sequence R
description binding site for residue S1P C 203
source : AC8

27) chain C
residue 72
type
sequence H
description binding site for residue HEM D 201
source : AC9

28) chain C
residue 72
type
sequence H
description binding site for residue S1P D 202
source : AD1

29) chain C
residue 108
type MOD_RES
sequence T
description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
source Swiss-Prot : SWS_FT_FI11

30) chain C
residue 134
type MOD_RES
sequence T
description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
source Swiss-Prot : SWS_FT_FI11

31) chain C
residue 137
type MOD_RES
sequence T
description N6-acetyllysine; alternate => ECO:0000269|PubMed:4531009
source Swiss-Prot : SWS_FT_FI11

32) chain C
residue 7
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569
source Swiss-Prot : SWS_FT_FI12

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

34) chain C
residue 40
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) valine; in Hb A1c => ECO:0000269|PubMed:635569
source Swiss-Prot : SWS_FT_FI12

35) chain C
residue 8
type BINDING
sequence T
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

36) chain C
residue 13
type BINDING
sequence A
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

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

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

39) chain C
residue 45
type BINDING
sequence H
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

40) chain C
residue 47
type BINDING
sequence D
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

41) chain C
residue 52
type BINDING
sequence S
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

42) chain C
residue 55
type BINDING
sequence V
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

43) chain C
residue 59
type BINDING
sequence G
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

44) chain C
residue 91
type BINDING
sequence L
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

45) chain C
residue 106
type BINDING
sequence L
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

46) chain C
residue 108
type BINDING
sequence T
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

47) chain C
residue 121
type BINDING
sequence V
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

48) chain C
residue 133
type BINDING
sequence S
description proximal binding residue
source Swiss-Prot : SWS_FT_FI3

49) chain C
residue 7
type MOD_RES
sequence K
description N-pyruvate 2-iminyl-valine; in Hb A1b
source Swiss-Prot : SWS_FT_FI6

50) chain C
residue 16
type MOD_RES
sequence K
description N-pyruvate 2-iminyl-valine; in Hb A1b
source Swiss-Prot : SWS_FT_FI6

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

52) chain C
residue 102
type MOD_RES
sequence S
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

53) chain C
residue 124
type MOD_RES
sequence S
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

54) chain C
residue 131
type MOD_RES
sequence S
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10

55) chain C
residue 138
type MOD_RES
sequence S
description S-nitrosocysteine => ECO:0000269|PubMed:8637569, ECO:0000269|PubMed:9843411
source Swiss-Prot : SWS_FT_FI10


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