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3ADE

Crystal Structure of Keap1 in Complex with Sequestosome-1/p62

Functional Information from GO Data
ChainGOidnamespacecontents
A0008134molecular_functiontranscription factor binding
A0016567biological_processprotein ubiquitination
A0031463cellular_componentCul3-RING ubiquitin ligase complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AARG442
AGLU444
AARG447

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AILE421
AASP422
AHIS424
ATYR426
AARG442
APRO492

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
AHIS451
ALEU452

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
AHIS424
AGLU444
APRO445
AGLU446
AARG447

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 705
ChainResidue
APRO361
AASN532
AHIS553

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 706
ChainResidue
ACYS406
AALA407
ASER408

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 707
ChainResidue
AILE435
AHIS436
AARG459
AASP479
AARG494
AARG498

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 708
ChainResidue
AHOH15
AHIS437
ASER438
ASER439
AARG494

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 709
ChainResidue
AARG326
AVAL561
AHIS562
AGLN563

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:24011591, ECO:0000269|PubMed:37306101
ChainResidueDetails
BSER351

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q13501
ChainResidueDetails
BSER357
ACYS613

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: S-cGMP-cysteine => ECO:0000269|PubMed:20498371
ChainResidueDetails
ACYS434

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PDB entries from 2024-05-01

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