eF-site ID 1e4h-A
PDB Code 1e4h
Chain A

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Title Structure of human transthyretin complexed with bromophenols: a new mode of binding
Classification TRANSPORT PROTEIN
Compound TRANSTHYRETIN
Source ORGANISM_COMMON: HUMAN; ORGANISM_SCIENTIFIC: HOMO SAPIENS;
Sequence A:  CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKT
SESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHE
HAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNP
Description


Functional site

1) chain A
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE PBR B 999
source : AC2

2) chain A
residue 15
type
sequence K
description BINDING SITE FOR RESIDUE PBR B 999
source : AC2

3) chain A
residue 119
type
sequence T
description BINDING SITE FOR RESIDUE PBR B 999
source : AC2

4) chain A
residue 119
type
sequence T
description BINDING SITE FOR RESIDUE PBR B 999
source : AC2

5) chain A
residue 41
type
sequence W
description BINDING SITE FOR RESIDUE GOL A 990
source : AC3

6) chain A
residue 70
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 990
source : AC3

7) chain A
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 990
source : AC3

8) chain A
residue 110
type
sequence L
description BINDING SITE FOR RESIDUE GOL B 990
source : AC4

9) chain A
residue 117
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 990
source : AC4

10) chain A
residue 117
type
sequence S
description BINDING SITE FOR RESIDUE GOL B 990
source : AC4

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

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

13) 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

14) 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

15) 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

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

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

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

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


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