Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5LHH

Structure of the KDM1A/CoREST complex with the inhibitor 4-ethyl-N-[3-(methoxymethyl)-2-[[4-[[(3R)-pyrrolidin-3-yl]methoxy]phenoxy]methyl]phenyl]thieno[3,2-b]pyrrole-5-carboxamide

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
A0006338biological_processchromatin remodeling
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
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
A0090308biological_processregulation of DNA methylation-dependent heterochromatin formation
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
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
B0000118cellular_componenthistone deacetylase complex
B0003682molecular_functionchromatin binding
B0003714molecular_functiontranscription corepressor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005667cellular_componenttranscription regulator complex
B0006325biological_processchromatin organization
B0006357biological_processregulation of transcription by RNA polymerase II
B0010629biological_processnegative regulation of gene expression
B0017053cellular_componenttranscription repressor complex
B0019899molecular_functionenzyme binding
B0030218biological_processerythrocyte differentiation
B0045654biological_processpositive regulation of megakaryocyte differentiation
B0045892biological_processnegative regulation of DNA-templated transcription
B1990391cellular_componentDNA repair complex
Functional Information from PDB Data
site_idAC1
Number of Residues43
Detailsbinding site for residue FAD A 901
ChainResidue
AGLY285
AGLY315
AARG316
AVAL317
ALEU329
AGLY330
AALA331
AMET332
AVAL333
ATHR588
AALA589
AGLY287
AVAL590
ATHR624
ALEU625
APRO626
AVAL637
ATRP751
ATRP756
ASER760
ATYR761
AGLY800
AVAL288
AGLU801
AALA809
ATHR810
AVAL811
AALA814
A6X0908
AHOH1002
AHOH1004
AHOH1012
AHOH1014
ASER289
AHOH1015
AHOH1018
AHOH1021
AHOH1029
ALEU307
AGLU308
AALA309
AARG310
AGLY314

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 902
ChainResidue
AARG310
AARG312
AARG750
ATRP751
AASP754
AGOL904

site_idAC3
Number of Residues10
Detailsbinding site for residue GOL A 903
ChainResidue
AVAL468
ALYS469
ALYS631
AGLN652
AARG653
AMET654
AGLY655
APHE656
ATYR763
AHOH1017

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 904
ChainResidue
AARG312
ATHR319
ALEU329
AGOL902

site_idAC5
Number of Residues3
Detailsbinding site for residue GOL A 905
ChainResidue
AGLU413
AARG526
AARG688

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 907
ChainResidue
ATHR335
AASP555
AHIS812

site_idAC7
Number of Residues12
Detailsbinding site for residue 6X0 A 908
ChainResidue
AVAL333
ATHR335
AGLN358
APHE538
AALA539
AASP555
AHIS564
ATRP695
ATYR761
AALA809
AFAD901
AHOH1021

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BARG127
AGLU308
AARG310
AARG316
AMET332
AGLU801
ATHR810

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BGLU260

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BASN460

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BARG122
BLYS297
BGLU466

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon