eF-site ID 3tdl-A
PDB Code 3tdl
Chain A

click to enlarge
Title Structure of human serum albumin in complex with DAUDA
Classification TRANSPORT PROTEIN
Compound Serum albumin
Source Homo sapiens (Human) (ALBU_HUMAN)
Sequence A:  HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKL
VNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRE
TYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDV
MCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYK
AAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCAS
LQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVH
TECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKP
LLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEA
KDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCA
AADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPE
AKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLV
NRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQ
IKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKET
CFAEEGKKLVAASQAALG
Description


Functional site
1) chain A
residue 10
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
2) chain A
residue 19
type
sequence F
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
3) chain A
residue 22
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
4) chain A
residue 23
type
sequence V
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
5) chain A
residue 66
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
6) chain A
residue 150
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
7) chain A
residue 152
type
sequence P
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
8) chain A
residue 250
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
9) chain A
residue 251
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
10) chain A
residue 254
type
sequence A
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
11) chain A
residue 257
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
12) chain A
residue 283
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
13) chain A
residue 284
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
14) chain A
residue 287
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1002
source : AC1
15) chain A
residue 342
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC2
16) chain A
residue 348
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC2
17) chain A
residue 391
type
sequence N
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC2
18) chain A
residue 485
type
sequence R
description BINDING SITE FOR RESIDUE MYR A 1003
source : AC2
19) chain A
residue 411
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC3
20) chain A
residue 430
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC3
21) chain A
residue 453
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC3
22) chain A
residue 488
type
sequence F
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC3
23) chain A
residue 489
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1004
source : AC3
24) chain A
residue 401
type
sequence Y
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
25) chain A
residue 405
type
sequence N
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
26) chain A
residue 507
type
sequence F
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
27) chain A
residue 525
type
sequence K
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
28) chain A
residue 528
type
sequence A
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
29) chain A
residue 532
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
30) chain A
residue 548
type
sequence M
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
31) chain A
residue 551
type
sequence F
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
32) chain A
residue 552
type
sequence A
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
33) chain A
residue 575
type
sequence L
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
34) chain A
residue 576
type
sequence V
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
35) chain A
residue 579
type
sequence S
description BINDING SITE FOR RESIDUE MYR A 1005
source : AC4
36) chain A
residue 209
type
sequence R
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
37) chain A
residue 212
type
sequence K
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
38) chain A
residue 213
type
sequence A
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
39) chain A
residue 324
type
sequence D
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
40) chain A
residue 325
type
sequence V
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
41) chain A
residue 327
type
sequence L
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
42) chain A
residue 328
type
sequence G
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
43) chain A
residue 351
type
sequence K
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
44) chain A
residue 480
type
sequence S
description BINDING SITE FOR RESIDUE 11D A 1006
source : AC5
45) chain A
residue 214
type
sequence W
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
46) chain A
residue 218
type
sequence R
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
47) chain A
residue 219
type
sequence L
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
48) chain A
residue 222
type
sequence R
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
49) chain A
residue 238
type
sequence L
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
50) chain A
residue 241
type
sequence V
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
51) chain A
residue 242
type
sequence H
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
52) chain A
residue 257
type
sequence R
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
53) chain A
residue 287
type
sequence S
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
54) chain A
residue 290
type
sequence I
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
55) chain A
residue 291
type
sequence A
description BINDING SITE FOR RESIDUE 11D A 1007
source : AC6
56) chain A
residue 161-185
type prosite
sequence YKAAFTECCQAADKAACLLPKLDEL
description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
source prosite : PS00212
57) chain A
residue 353-377
type prosite
sequence YETTLEKCCAAADPHECYAKVFDEF
description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
source prosite : PS00212
58) chain A
residue 551-575
type prosite
sequence FAAFVEKCCKETCFAEEGKKL
description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
source prosite : PS00212
59) chain A
residue 3
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P02770
source Swiss-Prot : SWS_FT_FI1
60) chain A
residue 83
type MOD_RES
sequence T
description Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI10
61) chain A
residue 205
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
62) chain A
residue 436
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
63) chain A
residue 519
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
64) chain A
residue 564
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI11
65) chain A
residue 273
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P07724
source Swiss-Prot : SWS_FT_FI12
66) chain A
residue 419
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI13
67) chain A
residue 420
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI14
68) chain A
residue 422
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI14
69) chain A
residue 489
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI15
70) chain A
residue 534
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI16
71) chain A
residue 12
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
72) chain A
residue 281
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
73) chain A
residue 317
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
74) chain A
residue 439
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI17
75) chain A
residue 51
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
76) chain A
residue 444
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
77) chain A
residue 536
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
78) chain A
residue 545
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
79) chain A
residue 573
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
80) chain A
residue 137
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
81) chain A
residue 162
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
82) chain A
residue 225
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
83) chain A
residue 276
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
84) chain A
residue 313
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
85) chain A
residue 323
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
86) chain A
residue 378
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
87) chain A
residue 413
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI18
88) chain A
residue 199
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480
source Swiss-Prot : SWS_FT_FI19
89) chain A
residue 6
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
90) chain A
residue 13
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
91) chain A
residue 244
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
92) chain A
residue 252
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
93) chain A
residue 255
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
94) chain A
residue 259
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P02769
source Swiss-Prot : SWS_FT_FI2
95) chain A
residue 233
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI20
96) chain A
residue 351
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI20
97) chain A
residue 318
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine; in variant Redhill
source Swiss-Prot : SWS_FT_FI21
98) chain A
residue 494
type CARBOHYD
sequence D
description N-linked (GlcNAc...) asparagine; in variant Casebrook
source Swiss-Prot : SWS_FT_FI22
99) chain A
residue 525
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480
source Swiss-Prot : SWS_FT_FI23
100) chain A
residue 534
type CARBOHYD
sequence K
description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977
source Swiss-Prot : SWS_FT_FI24
101) chain A
residue 67
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
102) chain A
residue 247
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
103) chain A
residue 249
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
source Swiss-Prot : SWS_FT_FI3
104) chain A
residue 240
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:656055
source Swiss-Prot : SWS_FT_FI4
105) chain A
residue 4
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
106) chain A
residue 174
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
107) chain A
residue 181
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
108) chain A
residue 190
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
109) chain A
residue 195
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
110) chain A
residue 205
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
111) chain A
residue 212
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
112) chain A
residue 240
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
113) chain A
residue 262
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
114) chain A
residue 274
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
115) chain A
residue 286
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
116) chain A
residue 20
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
117) chain A
residue 359
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
118) chain A
residue 372
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
119) chain A
residue 389
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
120) chain A
residue 402
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
121) chain A
residue 414
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
122) chain A
residue 432
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
123) chain A
residue 436
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
124) chain A
residue 466
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
125) chain A
residue 475
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
126) chain A
residue 500
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
127) chain A
residue 41
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
128) chain A
residue 519
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
129) chain A
residue 524
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
130) chain A
residue 538
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
131) chain A
residue 541
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
132) chain A
residue 557
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
133) chain A
residue 564
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
134) chain A
residue 574
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
135) chain A
residue 64
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
136) chain A
residue 73
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
137) chain A
residue 93
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
138) chain A
residue 106
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
139) chain A
residue 136
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
140) chain A
residue 159
type SITE
sequence K
description Not glycated => ECO:0000269|PubMed:15047055
source Swiss-Prot : SWS_FT_FI5
141) chain A
residue 199
type SITE
sequence K
description Aspirin-acetylated lysine
source Swiss-Prot : SWS_FT_FI6
142) chain A
residue 5
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI7
143) chain A
residue 58
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8
144) chain A
residue 65
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

Display surface

Download
Links