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5XMC

Crystal structure of the auto-inhibited Nedd4 family E3 ligase Itch

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0006511biological_processubiquitin-dependent protein catabolic process
A0061630molecular_functionubiquitin protein ligase activity
Functional Information from PROSITE/UniProt
site_idPS01159
Number of Residues26
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. Weqrvdqhgrv.YYvdhvekrTTWDRP
ChainResidueDetails
ATRP293-PRO318
ATRP325-PRO350
ATRP405-PRO430
ATRP445-PRO470

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00104
ChainResidueDetails
ACYS832

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK8 => ECO:0000269|PubMed:16446428
ChainResidueDetails
ASER199
ASER232

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK8 => ECO:0000269|PubMed:16446428
ChainResidueDetails
ATHR222

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by SGK3 => ECO:0000250|UniProtKB:Q96J02
ChainResidueDetails
ATHR346

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000250|UniProtKB:Q96J02
ChainResidueDetails
ATYR381

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by SGK3 => ECO:0000250|UniProtKB:Q96J02
ChainResidueDetails
ASER411

221051

PDB entries from 2024-06-12

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