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4DEU

Crystal Structure of the Wild Type TTR Binding Naringenin (TTRwt:NAR)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005179molecular_functionhormone activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0006144biological_processpurine nucleobase metabolic process
A0007165biological_processsignal transduction
A0035578cellular_componentazurophil granule lumen
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
A0070324molecular_functionthyroid hormone binding
B0005179molecular_functionhormone activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0006144biological_processpurine nucleobase metabolic process
B0007165biological_processsignal transduction
B0035578cellular_componentazurophil granule lumen
B0042802molecular_functionidentical protein binding
B0070062cellular_componentextracellular exosome
B0070324molecular_functionthyroid hormone binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 201
ChainResidue
APHE44
AGLU66
AASP99
AEDO202
AHOH369
AHOH410

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
AHOH410
AGLU66
AASP99
AEDO201

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
ASER23
APRO24
AVAL122
ATHR123
AEDO204
AHOH384
AHOH408

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 204
ChainResidue
APRO24
AILE26
AGLU51
AEDO203
AHOH357

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAR A 205
ChainResidue
ALYS15
ALYS15
ALEU17
ALEU17
AALA108
AALA108
ALEU110
ASER117
ATHR119
ATHR119
AHOH338
AHOH338
AHOH397
AHOH404
AHOH404
AHOH411
AHOH411
BSER115

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
AARG34
ASER46
AGLY47
AHIS56
AGLU66
AHOH311
AHOH383

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 207
ChainResidue
AASP74
ALYS76
ASER77
AGLU89
AHOH308
AHOH319
AHOH327

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 208
ChainResidue
AALA37
ALYS48
AGLU54
ALEU55
AHIS56
AHOH391

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 201
ChainResidue
BPHE44
BALA45
BGLY57
BLEU58
BGLU63
BGLU66
BASP99

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NAR B 202
ChainResidue
BLYS15
BLYS15
BLEU17
BALA108
BALA108
BLEU110
BSER117
BTHR119
BTHR119
BVAL121
BHOH393
BHOH397
BHOH407

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 203
ChainResidue
BSER46
BASN98

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 204
ChainResidue
BARG34
BLYS35
BGLY67
BILE68

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 205
ChainResidue
AHIS90
AGLU92
AHOH375
BTRP41
BLYS70
BGLU92
BHOH338
BHOH375

Functional Information from PROSITE/UniProt
site_idPS00768
Number of Residues16
DetailsTRANSTHYRETIN_1 Transthyretin signature 1. KVLDavrGsPAinVaV
ChainResidueDetails
ALYS15-VAL30

site_idPS00769
Number of Residues13
DetailsTRANSTHYRETIN_2 Transthyretin signature 2. YTIAalLSPYSYS
ChainResidueDetails
ATYR105-SER117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11418763, ECO:0007744|PDB:1ICT
ChainResidueDetails
ALYS15
AGLU54
ASER117
BLYS15
BGLU54
BSER117

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Sulfocysteine => ECO:0000269|PubMed:17175208, ECO:0007744|PDB:2H4E
ChainResidueDetails
ACYS10
BCYS10

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 4-carboxyglutamate; in a patient with Moyamoya disease => ECO:0000269|PubMed:18221012
ChainResidueDetails
AGLU42
BGLU42

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02767
ChainResidueDetails
ASER52
BSER52

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19167329
ChainResidueDetails
AASN98
BASN98

224201

PDB entries from 2024-08-28

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