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8FDV

LSD1-CoREST in complex N-formyl FAD and SNAG peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0002039molecular_functionp53 binding
A0002052biological_processpositive regulation of neuroblast proliferation
A0003682molecular_functionchromatin binding
A0003713molecular_functiontranscription coactivator activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005667cellular_componenttranscription regulator complex
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006482biological_processprotein demethylation
A0010569biological_processregulation of double-strand break repair via homologous recombination
A0010718biological_processpositive regulation of epithelial to mesenchymal transition
A0010976biological_processpositive regulation of neuron projection development
A0014070biological_processresponse to organic cyclic compound
A0016491molecular_functionoxidoreductase activity
A0019899molecular_functionenzyme binding
A0021987biological_processcerebral cortex development
A0030374molecular_functionnuclear receptor coactivator activity
A0031398biological_processpositive regulation of protein ubiquitination
A0032091biological_processnegative regulation of protein binding
A0032451molecular_functiondemethylase activity
A0032452molecular_functionhistone demethylase activity
A0032453molecular_functionhistone H3K4 demethylase activity
A0032454molecular_functionhistone H3K9 demethylase activity
A0032880biological_processregulation of protein localization
A0032991cellular_componentprotein-containing complex
A0034644biological_processcellular response to UV
A0036211biological_processprotein modification process
A0040029biological_processepigenetic regulation of gene expression
A0042162molecular_functiontelomeric DNA binding
A0042551biological_processneuron maturation
A0042802molecular_functionidentical protein binding
A0043392biological_processnegative regulation of DNA binding
A0043426molecular_functionMRF binding
A0043433biological_processnegative regulation of DNA-binding transcription factor activity
A0043518biological_processnegative regulation of DNA damage response, signal transduction by p53 class mediator
A0045793biological_processpositive regulation of cell size
A0045892biological_processnegative regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046098biological_processguanine metabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0050681molecular_functionnuclear androgen receptor binding
A0055001biological_processmuscle cell development
A0060765biological_processregulation of androgen receptor signaling pathway
A0060992biological_processresponse to fungicide
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0061752molecular_functiontelomeric repeat-containing RNA binding
A0071320biological_processcellular response to cAMP
A0071480biological_processcellular response to gamma radiation
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0140297molecular_functionDNA-binding transcription factor binding
A0140682molecular_functionFAD-dependent H3K4me/H3K4me3 demethylase activity
A0140861biological_processDNA repair-dependent chromatin remodeling
A0160217
A1902166biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
A1990391cellular_componentDNA repair complex
A1990841molecular_functionpromoter-specific chromatin binding
A2000179biological_processpositive regulation of neural precursor cell proliferation
A2000648biological_processpositive regulation of stem cell proliferation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4, ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO, ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D, ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF, ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH, ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ, ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48, ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1
ChainResidueDetails
ASER289
AGLU308
AARG310
AARG316
AMET332
AGLU801
ATHR810

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR59

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR104

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER126

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER131

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR135

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER137

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER166

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:27292636
ChainResidueDetails
ALYS432
ALYS433
ALYS436

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER611

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER849

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS442
ALYS469

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:25018020
ChainResidueDetails
ALYS503

227344

PDB entries from 2024-11-13

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