eF-site ID 2w72-C
PDB Code 2w72
Chain C

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Title DEOXYGENATED STRUCTURE OF A DISTAL SITE HEMOGLOBIN MUTANT PLUS XE
Classification OXYGEN TRANSPORT
Compound HUMAN HEMOGLOBIN A
Source (HBA_HUMAN)
Sequence C:  MLSPADKTNVKAAWGKVGAHAGEYGAEAYERMFLSFPTTK
TYFPHFDLSHGSAQVKGQGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKYR
Description


Functional site
1) chain C
residue 29
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
2) chain C
residue 42
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
3) chain C
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
4) chain C
residue 45
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
5) chain C
residue 46
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
6) chain C
residue 58
type
sequence Q
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
7) chain C
residue 61
type
sequence K
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
8) chain C
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
9) chain C
residue 83
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
10) chain C
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
11) chain C
residue 87
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
12) chain C
residue 91
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
13) chain C
residue 93
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
14) chain C
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
15) chain C
residue 98
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
16) chain C
residue 101
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
17) chain C
residue 136
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1142
source : AC3
18) chain C
residue 53
type
sequence A
description BINDING SITE FOR RESIDUE HEM D 1147
source : AC4
19) chain C
residue 36
type
sequence F
description BINDING SITE FOR RESIDUE SO4 C 1143
source : AC5
20) chain C
residue 37
type
sequence P
description BINDING SITE FOR RESIDUE SO4 C 1143
source : AC5
21) chain C
residue 38
type
sequence T
description BINDING SITE FOR RESIDUE SO4 C 1143
source : AC5
22) chain C
residue 119
type
sequence P
description BINDING SITE FOR RESIDUE SO4 D 1148
source : AC6
23) chain C
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 1149
source : AC9
24) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE SO4 C 1144
source : BC1
25) chain C
residue 127
type
sequence K
description BINDING SITE FOR RESIDUE SO4 C 1144
source : BC1
26) chain C
residue 130
type
sequence A
description BINDING SITE FOR RESIDUE SO4 C 1144
source : BC1
27) chain C
residue 141
type
sequence R
description BINDING SITE FOR RESIDUE PO4 C 1145
source : BC4
28) chain C
residue 14
type
sequence W
description BINDING SITE FOR RESIDUE XE C 1147
source : CC5
29) chain C
residue 128
type
sequence F
description BINDING SITE FOR RESIDUE XE C 1147
source : CC5
30) chain C
residue 33
type
sequence F
description BINDING SITE FOR RESIDUE XE C 1148
source : CC6
31) chain C
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE XE C 1148
source : CC6
32) chain C
residue 46
type
sequence F
description BINDING SITE FOR RESIDUE XE C 1148
source : CC6
33) chain C
residue 58
type
sequence Q
description BINDING SITE FOR RESIDUE XE C 1148
source : CC6
34) chain C
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE XE C 1149
source : CC7
35) chain C
residue 101
type
sequence L
description BINDING SITE FOR RESIDUE XE C 1149
source : CC7
36) chain C
residue 101
type
sequence L
description BINDING SITE FOR RESIDUE XE C 1150
source : CC8
37) chain C
residue 116
type
sequence E
description BINDING SITE FOR RESIDUE XE C 1151
source : CC9
38) chain C
residue 7
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI12
39) chain C
residue 16
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI12
40) chain C
residue 40
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI12
41) chain C
residue 61
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI13
42) chain C
residue 8
type SITE
sequence T
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
43) chain C
residue 13
type SITE
sequence A
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
44) chain C
residue 24
type SITE
sequence Y
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
45) chain C
residue 29
type SITE
sequence Y
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
46) chain C
residue 45
type SITE
sequence H
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
47) chain C
residue 47
type SITE
sequence D
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
48) chain C
residue 52
type SITE
sequence S
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
49) chain C
residue 55
type SITE
sequence V
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
50) chain C
residue 59
type SITE
sequence G
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
51) chain C
residue 91
type SITE
sequence L
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
52) chain C
residue 106
type SITE
sequence L
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
53) chain C
residue 108
type SITE
sequence T
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
54) chain C
residue 121
type SITE
sequence V
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
55) chain C
residue 133
type SITE
sequence S
description (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
source Swiss-Prot : SWS_FT_FI3
56) chain C
residue 11
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI4
57) chain C
residue 56
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI4
58) chain C
residue 60
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI4
59) chain C
residue 90
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI4
60) chain C
residue 99
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:7358733
source Swiss-Prot : SWS_FT_FI4
61) chain C
residue 3
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5
62) chain C
residue 35
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5
63) chain C
residue 49
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5
64) chain C
residue 7
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI6
65) chain C
residue 16
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI6
66) chain C
residue 40
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI6
67) chain C
residue 8
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7
68) chain C
residue 11
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI8
69) chain C
residue 24
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
70) chain C
residue 138
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI10
71) chain C
residue 102
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI10
72) chain C
residue 124
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI10
73) chain C
residue 131
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI10
74) chain C
residue 134
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI11
75) chain C
residue 137
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI11
76) chain C
residue 108
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P01942
source Swiss-Prot : SWS_FT_FI11
77) chain C
residue 58
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
source Swiss-Prot : SWS_FT_FI1
78) chain C
residue 87
type BINDING
sequence H
description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
source Swiss-Prot : SWS_FT_FI2

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