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6T36

Crystal structure of the PTPN3 PDZ domain bound to the HBV core protein C-terminal peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0001784molecular_functionphosphotyrosine residue binding
A0004721molecular_functionphosphoprotein phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006470biological_processprotein dephosphorylation
A0008092molecular_functioncytoskeletal protein binding
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016311biological_processdephosphorylation
A0017080molecular_functionsodium channel regulator activity
A0042059biological_processnegative regulation of epidermal growth factor receptor signaling pathway
A0045930biological_processnegative regulation of mitotic cell cycle
A0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
A0051117molecular_functionATPase binding
A0097421biological_processliver regeneration
A0098902biological_processregulation of membrane depolarization during action potential
A2000649biological_processregulation of sodium ion transmembrane transporter activity
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005198molecular_functionstructural molecule activity
B0005576cellular_componentextracellular region
B0019049biological_processvirus-mediated perturbation of host defense response
B0030430cellular_componenthost cell cytoplasm
B0039619cellular_componentT=4 icosahedral viral capsid
B0043657cellular_componenthost cell
B0046718biological_processsymbiont entry into host cell
B0075521biological_processmicrotubule-dependent intracellular transport of viral material towards nucleus
B0075732biological_processviral penetration into host nucleus
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue BR A 1001
ChainResidue
ALYS552

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHCsaGigRTG
ChainResidueDetails
AVAL840-GLY850

site_idPS00660
Number of Residues30
DetailsFERM_1 FERM domain signature 1. WLeasKaIrkQ..Lkggfpct.LhfrvrFFipD
ChainResidueDetails
ATRP84-ASP113

site_idPS00661
Number of Residues30
DetailsFERM_2 FERM domain signature 2. HeqhsglkqsEAescYIni.ArtLdfYGvEL
ChainResidueDetails
AHIS192-LEU221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000255|PROSITE-ProRule:PRU10044
ChainResidueDetails
ACYS842

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLN886
AASP811
ACYS842

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER357

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER359

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER367
ASER381

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR376

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER425

219869

PDB entries from 2024-05-15

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