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4HSU

Crystal structure of LSD2-NPAC with H3(1-26)in space group P21

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0000786cellular_componentnucleosome
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0032452molecular_functionhistone demethylase activity
A0032453molecular_functionhistone H3K4 demethylase activity
A0040029biological_processepigenetic regulation of gene expression
A0042393molecular_functionhistone binding
A0044726biological_processepigenetic programing of female pronucleus
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0071514biological_processgenomic imprinting
A0071949molecular_functionFAD binding
A0140682molecular_functionFAD-dependent H3K4me/H3K4me3 demethylase activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 901
ChainResidue
AILE388
AGLY419
AARG420
AARG434
AGLY435
AALA436
AILE438
AVAL598
AVAL627
APRO628
ATRP757
AGLY389
ATRP762
AALA766
AGLY794
AGLU795
AGLN803
ATHR804
AVAL805
AALA808
AHOH1108
AHOH1125
AGLY391
AHOH1127
AHOH1148
AHOH1188
APRO392
AALA393
ALEU411
AGLU412
AALA413
ALYS414

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
ACYS53
ACYS58
AHIS84
AHIS90

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 903
ChainResidue
ACYS65
ACYS73
ACYS92
ACYS95

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 904
ChainResidue
ACYS142
ACYS147
ACYS169
ACYS185

Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
CLYS14-LEU20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsDNA_BIND: A.T hook => ECO:0000305|PubMed:30970244
ChainResidueDetails
BPRO168-ASP180

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Required to promote KDM1B demethylase activity toward histone H3K4me1 and H3K4me2 => ECO:0000269|PubMed:23260659
ChainResidueDetails
BPHE217
AGLN803
ACYS58
ACYS65
ACYS73
AHIS84
AHIS90
ACYS92
ACYS95
AVAL598

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692
ChainResidueDetails
BSER167
ACYS147
ACYS169
ACYS185

site_idSWS_FT_FI4
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS176
BLYS179
BLYS201
BLYS211
BLYS240

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS227
BLYS237

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER247

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PDB entries from 2024-11-06

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