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5X54

Crystal structure of the Keap1 Kelch domain in complex with a tetrapeptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0008134molecular_functiontranscription factor binding
A0016567biological_processprotein ubiquitination
A0031463cellular_componentCul3-RING ubiquitin ligase complex
B0008134molecular_functiontranscription factor binding
B0016567biological_processprotein ubiquitination
B0031463cellular_componentCul3-RING ubiquitin ligase complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ACT B 901
ChainResidue
BTYR491
BPRO492
BGLU493
BARG494
BHOH1065

site_idAC2
Number of Residues2
Detailsbinding site for residue ACT B 902
ChainResidue
BASP357
BARG470

site_idAC3
Number of Residues11
Detailsbinding site for Di-peptide ACE C 0 and GLU C 1
ChainResidue
ASER508
AASP587
ATHR588
CTRP2
CTRP3
CTRP4
CHOH101
CHOH103
CHOH104
AARG415
AARG483

site_idAC4
Number of Residues7
Detailsbinding site for Di-peptide ACE D 0 and GLU D 1
ChainResidue
BARG415
BARG483
BSER508
DTRP2
DTRP3
DTRP4
DHOH101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Sensor for electrophilic agents => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
ACYS434
BCYS434

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: S-cGMP-cysteine => ECO:0000250|UniProtKB:Q9Z2X8
ChainResidueDetails
ACYS434
BCYS434

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PDB entries from 2024-07-24

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