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6VYP

Crystal structure of the LSD1/CoREST histone demethylase bound to its nucleosome substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
K0005634cellular_componentnucleus
K0006355biological_processregulation of DNA-templated transcription
K0016491molecular_functionoxidoreductase activity
K0050660molecular_functionflavin adenine dinucleotide binding
M0005634cellular_componentnucleus
M0006355biological_processregulation of DNA-templated transcription
M0016491molecular_functionoxidoreductase activity
M0050660molecular_functionflavin adenine dinucleotide binding
a0000786cellular_componentnucleosome
a0003677molecular_functionDNA binding
a0005515molecular_functionprotein binding
a0005634cellular_componentnucleus
a0005654cellular_componentnucleoplasm
a0005694cellular_componentchromosome
a0030527molecular_functionstructural constituent of chromatin
a0046982molecular_functionprotein heterodimerization activity
b0000786cellular_componentnucleosome
b0003677molecular_functionDNA binding
b0005515molecular_functionprotein binding
b0005634cellular_componentnucleus
b0005694cellular_componentchromosome
b0006334biological_processnucleosome assembly
b0030527molecular_functionstructural constituent of chromatin
b0046982molecular_functionprotein heterodimerization activity
c0000786cellular_componentnucleosome
c0003677molecular_functionDNA binding
c0005634cellular_componentnucleus
c0005694cellular_componentchromosome
c0030527molecular_functionstructural constituent of chromatin
c0046982molecular_functionprotein heterodimerization activity
d0000786cellular_componentnucleosome
d0003677molecular_functionDNA binding
d0005515molecular_functionprotein binding
d0005634cellular_componentnucleus
d0005694cellular_componentchromosome
d0030527molecular_functionstructural constituent of chromatin
d0046982molecular_functionprotein heterodimerization activity
e0000786cellular_componentnucleosome
e0003677molecular_functionDNA binding
e0005515molecular_functionprotein binding
e0005634cellular_componentnucleus
e0005654cellular_componentnucleoplasm
e0005694cellular_componentchromosome
e0030527molecular_functionstructural constituent of chromatin
e0046982molecular_functionprotein heterodimerization activity
f0000786cellular_componentnucleosome
f0003677molecular_functionDNA binding
f0005515molecular_functionprotein binding
f0005634cellular_componentnucleus
f0005694cellular_componentchromosome
f0006334biological_processnucleosome assembly
f0030527molecular_functionstructural constituent of chromatin
f0046982molecular_functionprotein heterodimerization activity
g0000786cellular_componentnucleosome
g0003677molecular_functionDNA binding
g0005634cellular_componentnucleus
g0005694cellular_componentchromosome
g0030527molecular_functionstructural constituent of chromatin
g0046982molecular_functionprotein heterodimerization activity
h0000786cellular_componentnucleosome
h0003677molecular_functionDNA binding
h0005515molecular_functionprotein binding
h0005634cellular_componentnucleus
h0005694cellular_componentchromosome
h0030527molecular_functionstructural constituent of chromatin
h0046982molecular_functionprotein heterodimerization activity
k0005634cellular_componentnucleus
k0006355biological_processregulation of DNA-templated transcription
k0016491molecular_functionoxidoreductase activity
k0050660molecular_functionflavin adenine dinucleotide binding
m0005634cellular_componentnucleus
m0006355biological_processregulation of DNA-templated transcription
m0016491molecular_functionoxidoreductase activity
m0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue FAD M 900
ChainResidue
EMET4
MGLY315
MARG316
MVAL317
MGLY330
MALA331
MVAL333
MVAL590
MTHR624
MLEU625
MPRO626
MGLY285
MLEU659
MTRP756
MSER760
MTYR761
MGLY800
MGLU801
MTHR810
MVAL811
MALA814
MGLY287
MVAL288
MSER289
MGLU308
MALA309
MARG310
MGLY314

site_idAC2
Number of Residues31
Detailsbinding site for Di-peptide FAD K 900 and ARG K 310
ChainResidue
KGLY285
KGLY287
KVAL288
KSER289
KLEU307
KGLU308
KALA309
KASP311
KARG312
KGLY314
KGLY315
KARG316
KGLY330
KALA331
KMET332
KVAL333
KVAL334
KLEU586
KASN587
KTHR624
KLEU625
KASP754
KTRP756
KSER760
KTYR761
KGLY800
KGLU801
KALA809
KTHR810
KVAL811
KALA814

site_idAC3
Number of Residues29
Detailsbinding site for Di-peptide FAD K 900 and GLY K 315
ChainResidue
KGLY285
KGLY287
KVAL288
KSER289
KLEU307
KGLU308
KALA309
KARG310
KARG312
KVAL313
KGLY314
KARG316
KVAL317
KGLY330
KALA331
KMET332
KVAL333
KVAL334
KTHR624
KLEU625
KTRP756
KSER760
KTYR761
KGLY800
KGLU801
KALA809
KTHR810
KVAL811
KALA814

site_idAC4
Number of Residues29
Detailsbinding site for Di-peptide FAD K 900 and GLY K 330
ChainResidue
KASP328
KLEU329
KALA331
KMET332
KVAL333
KVAL334
KTHR624
KLEU625
KTRP751
KTRP756
KSER760
KTYR761
KGLY800
KGLU801
KALA809
KTHR810
KVAL811
KALA814
KGLY285
KGLY287
KVAL288
KSER289
KLEU307
KGLU308
KALA309
KARG310
KGLY314
KGLY315
KARG316

site_idAC5
Number of Residues28
Detailsbinding site for Di-peptide FAD K 900 and VAL K 333
ChainResidue
KGLY285
KGLY287
KVAL288
KSER289
KLEU307
KGLU308
KALA309
KARG310
KGLY314
KGLY315
KARG316
KGLY330
KALA331
KMET332
KVAL334
KLEU565
KTHR566
KTHR624
KLEU625
KTRP756
KSER760
KTYR761
KGLY800
KGLU801
KALA809
KTHR810
KVAL811
KALA814

site_idAC6
Number of Residues29
Detailsbinding site for Di-peptide FAD k 900 and ALA k 331
ChainResidue
kGLY285
kSER286
kGLY287
kVAL288
kSER289
kGLU308
kALA309
kARG310
kGLY314
kGLY315
kARG316
kGLY330
kMET332
kVAL333
kVAL590
kTHR624
kLEU625
kPRO626
kVAL629
kLEU659
kTRP756
kSER760
kTYR761
kGLY800
kGLU801
kTHR810
kVAL811
kHIS812
kALA814

site_idAC7
Number of Residues31
Detailsbinding site for Di-peptide FAD k 900 and VAL k 811
ChainResidue
kGLY285
kSER286
kGLY287
kVAL288
kSER289
kGLU308
kALA309
kARG310
kGLY314
kGLY315
kARG316
kALA331
kMET332
kVAL333
kTYR571
kVAL590
kTHR624
kLEU625
kPRO626
kVAL629
kLEU659
kTRP756
kSER760
kTYR761
kGLY800
kGLU801
kTHR810
kHIS812
kGLY813
kALA814
kLEU815

site_idAC8
Number of Residues34
Detailsbinding site for Di-peptide FAD k 900 and HIS k 812
ChainResidue
kGLY285
kSER286
kGLY287
kVAL288
kSER289
kGLU308
kALA309
kARG310
kGLY314
kGLY315
kARG316
kALA331
kMET332
kVAL333
kTHR335
kASN340
kMET342
kVAL590
kTHR624
kLEU625
kPRO626
kVAL629
kLEU659
kTRP756
kSER760
kTYR761
kGLY800
kGLU801
kTHR810
kVAL811
kGLY813
kALA814
kLEU815
kLEU816

site_idAC9
Number of Residues33
Detailsbinding site for Di-peptide FAD k 900 and ALA k 814
ChainResidue
kGLY285
kSER286
kGLY287
kVAL288
kSER289
kGLU308
kALA309
kARG310
kGLY314
kGLY315
kARG316
kALA331
kMET332
kVAL333
kVAL590
kTHR624
kLEU625
kPRO626
kVAL629
kLEU659
kTRP756
kSER760
kTYR761
kGLY800
kGLU801
kTHR810
kVAL811
kHIS812
kGLY813
kLEU815
kLEU816
kSER817
kGLY818

site_idAD1
Number of Residues29
Detailsbinding site for Di-peptide FAD m 900 and GLY m 330
ChainResidue
mGLY285
mSER286
mGLY287
mVAL288
mSER289
mGLU308
mALA309
mARG310
mGLY314
mGLY315
mARG316
mVAL317
mALA318
mASP328
mLEU329
mALA331
mVAL333
mVAL590
mTHR624
mLEU625
mPRO626
mLYS661
mTRP751
mTRP756
mGLY800
mGLU801
mTHR810
mVAL811
mALA814

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
KARG310
KARG316
KMET332
KGLU801
KTHR810
kSER289
kGLU308
kARG310
kARG316
kMET332
kGLU801
kTHR810
AARG2
AARG17
EARG2
EARG17
aARG2
aARG17
eARG2
eARG17
mGLU308
mARG310
mARG316
mMET332
mGLU801
mTHR810
KSER289
KGLU308

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR3
ETHR3
aTHR3
eTHR3

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181
ChainResidueDetails
AMET4
EMET4
aMET4
eMET4
cLYS9
cLYS95
gLYS9
gLYS95

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
KLYS469
kLYS469
AGLN5
EGLN5
aGLN5
eGLN5
KLYS442
kLYS442

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR6
ATHR11
ETHR6
ETHR11
aTHR6
aTHR11
eTHR6
eTHR11
bLYS8
bLYS16
bLYS44
bLYS79
fLYS8
fLYS16
fLYS44
fLYS79

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250
ChainResidueDetails
AARG8
EARG8
aARG8
eARG8
bLYS12
bLYS20
fLYS12
fLYS20

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181
ChainResidueDetails
ALYS9
ELYS9
aLYS9
eLYS9
bLYS31
bLYS91
fLYS31
fLYS91

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
gLYS13
gLYS15
gLYS119
ASER10
ESER10
aSER10
eSER10
GLYS13
GLYS15
GLYS119
cLYS13
cLYS15
cLYS119

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ALYS14
ELYS14
aLYS14
eLYS14
bTYR51
bTYR88
fTYR51
fTYR88

site_idSWS_FT_FI10
Number of Residues20
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ELYS64
aLYS18
aLYS23
aLYS27
aLYS36
aLYS64
eLYS18
eLYS23
eLYS27
eLYS36
eLYS64
ALYS64
ELYS18
ELYS23
ELYS27
ELYS36
ALYS18
ALYS23
ALYS27
ALYS36

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AARG26
EARG26
aARG26
eARG26

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER28
ESER28
aSER28
eSER28

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
bLYS91
fLYS91
ALYS37
ELYS37
aLYS37
eLYS37

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATYR41
ETYR41
aTYR41
eTYR41

site_idSWS_FT_FI15
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
aLYS56
aLYS79
eLYS56
eLYS79
ALYS56
ALYS79
ELYS56
ELYS79

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER57
ESER57
aSER57
eSER57

site_idSWS_FT_FI17
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
aTHR80
aTHR107
eTHR80
eTHR107
ATHR80
ATHR107
ETHR80
ETHR107

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86
aSER86
eSER86

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS115
ELYS115
aLYS115
eLYS115

site_idSWS_FT_FI20
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS122
ELYS122
aLYS122
eLYS122

site_idSWS_FT_FI21
Number of Residues4
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ACYS110
ECYS110
aCYS110
eCYS110

218853

PDB entries from 2024-04-24

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