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4GUT

Crystal structure of LSD2-NPAC

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0032452molecular_functionhistone demethylase activity
A0032453molecular_functionhistone H3K4 demethylase activity
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
Functional Information from PDB Data
site_idAC1
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 901
ChainResidue
AILE388
AGLY419
AARG420
AARG434
AGLY435
AALA436
AGLN437
AILE438
AVAL598
AVAL627
APRO628
AGLY389
AILE637
ATRP757
ATRP762
AALA766
AGLY794
AGLU795
AGLN803
ATHR804
AVAL805
AALA808
AGLY391
AGOL902
AHOH1103
AHOH1106
AHOH1116
AHOH1126
AHOH1266
AHOH1434
APRO392
AALA393
ALEU411
AGLU412
AALA413
ALYS414

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 902
ChainResidue
AALA546
ATYR767
AGLN803
ATHR804
AFAD901
AHOH1266

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 903
ChainResidue
ATRP422
AARG434
ATHR755
AARG756
ATRP757

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 904
ChainResidue
ACYS53
ACYS58
AHIS84
AHIS90

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 905
ChainResidue
ACYS65
ACYS73
ACYS92
ACYS95

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 906
ChainResidue
ACYS142
ACYS147
ACYS169
ACYS185

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PGE B 301
ChainResidue
ATYR223
ATYR273
AGLN274
AASN276
AGLU277
AARG285
AASP287
BPHE217
BHIS218

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 2024-09-11

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