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2Z32

Crystal structure of Keap1 complexed with Prothymosin alpha

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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AHOH62
AGLY325
AHIS562
AGLN563

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AASN532
AHIS553
AHOH64
AHOH187
AHOH199
AHOH218
AGLN359

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 703
ChainResidue
AHOH56
AHOH165
ACYS434
AILE435
AHIS436
AARG459
AARG494
AARG498

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 704
ChainResidue
AHOH17
AHOH68
AHOH95
AHOH161
AHIS437
ASER438
ASER439
AARG494

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 705
ChainResidue
AHOH130
AHOH217
AILE421
AASP422
AHIS424
ATYR426
AARG442
APRO492

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Sensor for electrophilic agents => ECO:0000269|PubMed:20498371
ChainResidueDetails
ACYS434

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: S-(2-succinyl)cysteine => ECO:0000269|PubMed:22014577
ChainResidueDetails
ACYS319
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 2024-07-31

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