eF-site ID 4i87-AB
PDB Code 4i87
Chain A, B

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Title Crystal structure of TTR variant I84S in complex with CHF5074 at acidic pH
Classification transport protein/inhibitor
Compound Transthyretin
Source Homo sapiens (Human) (TTHY_HUMAN)
Sequence A:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT
SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGSSPFHE
HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP
B:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT
SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGSSPFHE
HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN
Description


Functional site

1) chain A
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

2) chain A
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

3) chain A
residue 17
type
sequence L
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

4) chain A
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

5) chain A
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

6) chain A
residue 109
type
sequence A
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

7) chain A
residue 110
type
sequence L
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

8) chain A
residue 117
type
sequence S
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

9) chain A
residue 117
type
sequence S
description BINDING SITE FOR RESIDUE H50 A 201
source : AC1

10) chain B
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

11) chain B
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

12) chain B
residue 17
type
sequence L
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

13) chain B
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

14) chain B
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

15) chain B
residue 110
type
sequence L
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

16) chain B
residue 117
type
sequence S
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

17) chain B
residue 117
type
sequence S
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

18) chain B
residue 118
type
sequence T
description BINDING SITE FOR RESIDUE H50 B 201
source : AC2

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

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

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

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

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

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

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

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

27) 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

28) 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

29) 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

30) 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

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

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

33) 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

34) 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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