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5TV1

active arrestin-3 with inositol hexakisphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000822molecular_functioninositol hexakisphosphate binding
A0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
A0002031biological_processG protein-coupled receptor internalization
A0002092biological_processpositive regulation of receptor internalization
A0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005905cellular_componentclathrin-coated pit
A0007165biological_processsignal transduction
A0009968biological_processnegative regulation of signal transduction
A0015031biological_processprotein transport
A0030139cellular_componentendocytic vesicle
A0031410cellular_componentcytoplasmic vesicle
A0031623biological_processreceptor internalization
A0031701molecular_functionangiotensin receptor binding
A0035091molecular_functionphosphatidylinositol binding
A0060090molecular_functionmolecular adaptor activity
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue IHP A 401
ChainResidue
AARG104
ALYS108
ATHR226
ALYS227
AARG332
AHOH501

site_idAC2
Number of Residues7
Detailsbinding site for residue IHP A 402
ChainResidue
ALYS251
ALYS325
ALYS327
AGOL403
ALYS161
ALYS233
AARG237

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
ALYS12
ALYS295
AIHP402

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 404
ChainResidue
AGLN182
ASER184

site_idAC5
Number of Residues2
Detailsbinding site for residue GOL A 405
ChainResidue
APRO179
AGLY180

Functional Information from PROSITE/UniProt
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLsFrKDL
ChainResidueDetails
APHE62-LEU80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q91YI4
ChainResidueDetails
ATYR48

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Hydroxyproline; by PHD2 => ECO:0000250
ChainResidueDetails
APRO176
APRO181

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P29067
ChainResidueDetails
ASER360

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P29067
ChainResidueDetails
AARG393

222415

PDB entries from 2024-07-10

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