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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9V0A

Cryo-EM structure of pomalidomide-organized CRL4-DDB1-CRBN-IKZF3(ZF2-ZF3)-UbcH5a-Ub ubiquitylation assembly

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000109cellular_componentnucleotide-excision repair complex
A0001701biological_processin utero embryonic development
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006289biological_processnucleotide-excision repair
A0006974biological_processDNA damage response
A0007283biological_processspermatogenesis
A0008283biological_processcell population proliferation
A0010506biological_processregulation of autophagy
A0016567biological_processprotein ubiquitination
A0030174biological_processregulation of DNA-templated DNA replication initiation
A0031297biological_processreplication fork processing
A0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0032502biological_processdevelopmental process
A0032814biological_processregulation of natural killer cell activation
A0034644biological_processcellular response to UV
A0040029biological_processepigenetic regulation of gene expression
A0042110biological_processT cell activation
A0042127biological_processregulation of cell population proliferation
A0042254biological_processribosome biogenesis
A0042981biological_processregulation of apoptotic process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0045732biological_processpositive regulation of protein catabolic process
A0045995biological_processregulation of embryonic development
A0051246biological_processregulation of protein metabolic process
A0060964biological_processregulation of miRNA-mediated gene silencing
A0061630molecular_functionubiquitin protein ligase activity
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
A0080135biological_processregulation of cellular response to stress
A0097193biological_processintrinsic apoptotic signaling pathway
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1901987biological_processregulation of cell cycle phase transition
A1902412biological_processregulation of mitotic cytokinesis
A1904178biological_processnegative regulation of adipose tissue development
A2000036biological_processregulation of stem cell population maintenance
B0000109cellular_componentnucleotide-excision repair complex
B0000781cellular_componentchromosome, telomeric region
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006974biological_processDNA damage response
B0007056biological_processspindle assembly involved in female meiosis
B0007283biological_processspermatogenesis
B0008283biological_processcell population proliferation
B0010498biological_processproteasomal protein catabolic process
B0010506biological_processregulation of autophagy
B0016567biological_processprotein ubiquitination
B0019076biological_processviral release from host cell
B0030174biological_processregulation of DNA-templated DNA replication initiation
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031297biological_processreplication fork processing
B0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
B0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
B0032814biological_processregulation of natural killer cell activation
B0032991cellular_componentprotein-containing complex
B0034644biological_processcellular response to UV
B0035861cellular_componentsite of double-strand break
B0040029biological_processepigenetic regulation of gene expression
B0042127biological_processregulation of cell population proliferation
B0042752biological_processregulation of circadian rhythm
B0042981biological_processregulation of apoptotic process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044725biological_processepigenetic programming in the zygotic pronuclei
B0044877molecular_functionprotein-containing complex binding
B0045070biological_processpositive regulation of viral genome replication
B0045722biological_processpositive regulation of gluconeogenesis
B0045732biological_processpositive regulation of protein catabolic process
B0045995biological_processregulation of embryonic development
B0046726biological_processpositive regulation by virus of viral protein levels in host cell
B0051702biological_processbiological process involved in interaction with symbiont
B0060964biological_processregulation of miRNA-mediated gene silencing
B0070062cellular_componentextracellular exosome
B0070914biological_processUV-damage excision repair
B0071987molecular_functionWD40-repeat domain binding
B0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0080135biological_processregulation of cellular response to stress
B0097602molecular_functioncullin family protein binding
B0160072molecular_functionubiquitin ligase complex scaffold activity
B1901987biological_processregulation of cell cycle phase transition
B1901990biological_processregulation of mitotic cell cycle phase transition
B1902412biological_processregulation of mitotic cytokinesis
B1904178biological_processnegative regulation of adipose tissue development
B2000036biological_processregulation of stem cell population maintenance
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0016020cellular_componentmembrane
C0016567biological_processprotein ubiquitination
C0030177biological_processpositive regulation of Wnt signaling pathway
C0031333biological_processnegative regulation of protein-containing complex assembly
C0031334biological_processpositive regulation of protein-containing complex assembly
C0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
C0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
C0034766biological_processnegative regulation of monoatomic ion transmembrane transport
C0035641biological_processlocomotory exploration behavior
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0044325molecular_functiontransmembrane transporter binding
C0048471cellular_componentperinuclear region of cytoplasm
C1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000209biological_processprotein polyubiquitination
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0016567biological_processprotein ubiquitination
D0030514biological_processnegative regulation of BMP signaling pathway
D0031398biological_processpositive regulation of protein ubiquitination
D0032991cellular_componentprotein-containing complex
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0061630molecular_functionubiquitin protein ligase activity
D0061631molecular_functionubiquitin conjugating enzyme activity
D0070936biological_processprotein K48-linked ubiquitination
D1904262biological_processnegative regulation of TORC1 signaling
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005737cellular_componentcytoplasm
N0005829cellular_componentcytosol
N0006508biological_processproteolysis
N0006511biological_processubiquitin-dependent protein catabolic process
N0009653biological_processanatomical structure morphogenesis
N0016567biological_processprotein ubiquitination
N0019941biological_processmodification-dependent protein catabolic process
N0030162biological_processregulation of proteolysis
N0031386molecular_functionprotein tag activity
N0031625molecular_functionubiquitin protein ligase binding
N0036211biological_processprotein modification process
N0045116biological_processprotein neddylation
N0070062cellular_componentextracellular exosome
N0072757biological_processcellular response to camptothecin
R0000082biological_processG1/S transition of mitotic cell cycle
R0000109cellular_componentnucleotide-excision repair complex
R0000122biological_processnegative regulation of transcription by RNA polymerase II
R0000165biological_processMAPK cascade
R0000209biological_processprotein polyubiquitination
R0004842molecular_functionubiquitin-protein transferase activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005654cellular_componentnucleoplasm
R0005737cellular_componentcytoplasm
R0005794cellular_componentGolgi apparatus
R0005813cellular_componentcentrosome
R0005829cellular_componentcytosol
R0006283biological_processtranscription-coupled nucleotide-excision repair
R0006289biological_processnucleotide-excision repair
R0006355biological_processregulation of DNA-templated transcription
R0006511biological_processubiquitin-dependent protein catabolic process
R0006513biological_processprotein monoubiquitination
R0006879biological_processintracellular iron ion homeostasis
R0006974biological_processDNA damage response
R0007283biological_processspermatogenesis
R0007346biological_processregulation of mitotic cell cycle
R0008283biological_processcell population proliferation
R0010506biological_processregulation of autophagy
R0010564biological_processregulation of cell cycle process
R0010824biological_processregulation of centrosome duplication
R0014033biological_processneural crest cell differentiation
R0016485biological_processprotein processing
R0016567biological_processprotein ubiquitination
R0019005cellular_componentSCF ubiquitin ligase complex
R0019788molecular_functionNEDD8 transferase activity
R0030174biological_processregulation of DNA-templated DNA replication initiation
R0030510biological_processregulation of BMP signaling pathway
R0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
R0031297biological_processreplication fork processing
R0031461cellular_componentcullin-RING ubiquitin ligase complex
R0031462cellular_componentCul2-RING ubiquitin ligase complex
R0031463cellular_componentCul3-RING ubiquitin ligase complex
R0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
R0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
R0031466cellular_componentCul5-RING ubiquitin ligase complex
R0031467cellular_componentCul7-RING ubiquitin ligase complex
R0031625molecular_functionubiquitin protein ligase binding
R0032006biological_processregulation of TOR signaling
R0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
R0032480biological_processnegative regulation of type I interferon production
R0032814biological_processregulation of natural killer cell activation
R0034450molecular_functionubiquitin-ubiquitin ligase activity
R0034599biological_processcellular response to oxidative stress
R0034644biological_processcellular response to UV
R0040029biological_processepigenetic regulation of gene expression
R0042110biological_processT cell activation
R0042127biological_processregulation of cell population proliferation
R0042752biological_processregulation of circadian rhythm
R0042770biological_processsignal transduction in response to DNA damage
R0042981biological_processregulation of apoptotic process
R0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
R0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
R0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
R0043687biological_processpost-translational protein modification
R0044314biological_processprotein K27-linked ubiquitination
R0045116biological_processprotein neddylation
R0045724biological_processpositive regulation of cilium assembly
R0045732biological_processpositive regulation of protein catabolic process
R0045879biological_processnegative regulation of smoothened signaling pathway
R0045995biological_processregulation of embryonic development
R0046627biological_processnegative regulation of insulin receptor signaling pathway
R0050727biological_processregulation of inflammatory response
R0051298biological_processcentrosome duplication
R0051726biological_processregulation of cell cycle
R0060090molecular_functionmolecular adaptor activity
R0060173biological_processlimb development
R0060271biological_processcilium assembly
R0060964biological_processregulation of miRNA-mediated gene silencing
R0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
R0061630molecular_functionubiquitin protein ligase activity
R0061663molecular_functionNEDD8 ligase activity
R0062197biological_processcellular response to chemical stress
R0070534biological_processprotein K63-linked ubiquitination
R0070936biological_processprotein K48-linked ubiquitination
R0071230biological_processcellular response to amino acid stimulus
R0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
R0080135biological_processregulation of cellular response to stress
R0090090biological_processnegative regulation of canonical Wnt signaling pathway
R0090734cellular_componentsite of DNA damage
R0097602molecular_functioncullin family protein binding
R0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
R0160240biological_processRNA polymerase II transcription initiation surveillance
R0160276biological_processnegative regulation of beige fat cell differentiation
R1900076biological_processregulation of cellular response to insulin stimulus
R1901524biological_processregulation of mitophagy
R1901525biological_processnegative regulation of mitophagy
R1901987biological_processregulation of cell cycle phase transition
R1902412biological_processregulation of mitotic cytokinesis
R1902499biological_processpositive regulation of protein autoubiquitination
R1902883biological_processnegative regulation of response to oxidative stress
R1904178biological_processnegative regulation of adipose tissue development
R1904263biological_processpositive regulation of TORC1 signaling
R1904415biological_processregulation of xenophagy
R1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
R2000001biological_processregulation of DNA damage checkpoint
R2000036biological_processregulation of stem cell population maintenance
R2000104biological_processnegative regulation of DNA-templated DNA replication
Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues21
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cnq..CgasFtqkgnllrHicl..H
ChainResidueDetails
ICYS148-HIS168
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
DTYR74-LEU89
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD
ChainResidueDetails
NLYS27-ASP52
ULYS27-ASP52
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. LKkrIesLIDRdYMeRdkdnpnqYhYvA
ChainResidueDetails
ALEU732-ALA759
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues238
DetailsDomain: {"description":"Lon N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01123","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25108355","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4TZ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsRegion: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"(Microbial infection) Deamidated glutamine","evidences":[{"source":"PubMed","id":"20688984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23175788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23589306","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26632597","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PubMed","id":"38316879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylglycine","evidences":[{"source":"PubMed","id":"28525742","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues316
DetailsRegion: {"description":"WD repeat beta-propeller B; Interaction with CUL4A"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9ESW0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)","evidences":[{"source":"PubMed","id":"38316879","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DPL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DPL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z8B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11961546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38605244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1LDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1U6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HYE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F52","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4P5O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8Q7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8RHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

257179

PDB entries from 2026-07-29

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