eF-site ID 4wnj-AB
PDB Code 4wnj
Chain A, B

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Title Crystal structure of Transthyretin-quercetin complex
Classification TRANSPORT PROTEIN
Compound Transthyretin
Source Homo sapiens (Human) (TTHY_HUMAN)
Sequence A:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT
SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE
HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP
B:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT
SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE
HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN
Description


Functional site

1) chain A
residue 72
type
sequence E
description binding site for residue DMS A 201
source : AC1

2) chain A
residue 90
type
sequence H
description binding site for residue DMS A 201
source : AC1

3) chain A
residue 92
type
sequence E
description binding site for residue DMS A 201
source : AC1

4) chain B
residue 35
type
sequence K
description binding site for residue DMS A 201
source : AC1

5) chain B
residue 15
type
sequence K
description binding site for residue QUE B 201
source : AC2

6) chain B
residue 17
type
sequence L
description binding site for residue QUE B 201
source : AC2

7) chain B
residue 17
type
sequence L
description binding site for residue QUE B 201
source : AC2

8) chain B
residue 108
type
sequence A
description binding site for residue QUE B 201
source : AC2

9) chain B
residue 110
type
sequence L
description binding site for residue QUE B 201
source : AC2

10) chain B
residue 110
type
sequence L
description binding site for residue QUE B 201
source : AC2

11) chain B
residue 117
type
sequence S
description binding site for residue QUE B 201
source : AC2

12) chain B
residue 117
type
sequence S
description binding site for residue QUE B 201
source : AC2

13) chain B
residue 119
type
sequence T
description binding site for residue QUE B 201
source : AC2

14) chain B
residue 119
type
sequence T
description binding site for residue QUE B 201
source : AC2

15) chain A
residue 41
type
sequence W
description binding site for residue DMS B 202
source : AC3

16) chain B
residue 72
type
sequence E
description binding site for residue DMS B 202
source : AC3

17) chain B
residue 90
type
sequence H
description binding site for residue DMS B 202
source : AC3

18) chain A
residue 15-30
type prosite
sequence KVLDAVRGSPAINVAV
description TRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV
source prosite : PS00768

19) chain A
residue 105-117
type prosite
sequence YTIAALLSPYSYS
description TRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS
source prosite : PS00769

20) chain A
residue 15
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 54
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 117
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 15
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 54
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 117
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 10
type MOD_RES
sequence C
description Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 10
type MOD_RES
sequence C
description Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 42
type MOD_RES
sequence E
description 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
source Swiss-Prot : SWS_FT_FI3

29) chain B
residue 42
type MOD_RES
sequence E
description 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
source Swiss-Prot : SWS_FT_FI3

30) chain A
residue 52
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P02767
source Swiss-Prot : SWS_FT_FI4

31) chain B
residue 52
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P02767
source Swiss-Prot : SWS_FT_FI4

32) chain A
residue 98
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
source Swiss-Prot : SWS_FT_FI5

33) chain B
residue 98
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
source Swiss-Prot : SWS_FT_FI5


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