Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6VYP

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

Functional Information from GO Data

Chain	GOid	namespace	contents
a	0000786	cellular_component	nucleosome
a	0003677	molecular_function	DNA binding
a	0005515	molecular_function	protein binding
a	0005634	cellular_component	nucleus
a	0005654	cellular_component	nucleoplasm
a	0005694	cellular_component	chromosome
a	0030527	molecular_function	structural constituent of chromatin
a	0031492	molecular_function	nucleosomal DNA binding
a	0031507	biological_process	heterochromatin formation
a	0046982	molecular_function	protein heterodimerization activity
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0030527	molecular_function	structural constituent of chromatin
A	0031492	molecular_function	nucleosomal DNA binding
A	0031507	biological_process	heterochromatin formation
A	0046982	molecular_function	protein heterodimerization activity
b	0000786	cellular_component	nucleosome
b	0003677	molecular_function	DNA binding
b	0005515	molecular_function	protein binding
b	0005634	cellular_component	nucleus
b	0005694	cellular_component	chromosome
b	0006334	biological_process	nucleosome assembly
b	0030527	molecular_function	structural constituent of chromatin
b	0031507	biological_process	heterochromatin formation
b	0046982	molecular_function	protein heterodimerization activity
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0006334	biological_process	nucleosome assembly
B	0030527	molecular_function	structural constituent of chromatin
B	0031507	biological_process	heterochromatin formation
B	0046982	molecular_function	protein heterodimerization activity
c	0000786	cellular_component	nucleosome
c	0003677	molecular_function	DNA binding
c	0005634	cellular_component	nucleus
c	0005694	cellular_component	chromosome
c	0030527	molecular_function	structural constituent of chromatin
c	0031507	biological_process	heterochromatin formation
c	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0030527	molecular_function	structural constituent of chromatin
C	0031507	biological_process	heterochromatin formation
C	0046982	molecular_function	protein heterodimerization activity
d	0000786	cellular_component	nucleosome
d	0002227	biological_process	innate immune response in mucosa
d	0003677	molecular_function	DNA binding
d	0005515	molecular_function	protein binding
d	0005615	cellular_component	extracellular space
d	0005634	cellular_component	nucleus
d	0005694	cellular_component	chromosome
d	0006325	biological_process	chromatin organization
d	0019731	biological_process	antibacterial humoral response
d	0030527	molecular_function	structural constituent of chromatin
d	0031507	biological_process	heterochromatin formation
d	0046982	molecular_function	protein heterodimerization activity
d	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
D	0000786	cellular_component	nucleosome
D	0002227	biological_process	innate immune response in mucosa
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0006325	biological_process	chromatin organization
D	0019731	biological_process	antibacterial humoral response
D	0030527	molecular_function	structural constituent of chromatin
D	0031507	biological_process	heterochromatin formation
D	0046982	molecular_function	protein heterodimerization activity
D	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
e	0000786	cellular_component	nucleosome
e	0003677	molecular_function	DNA binding
e	0005515	molecular_function	protein binding
e	0005634	cellular_component	nucleus
e	0005654	cellular_component	nucleoplasm
e	0005694	cellular_component	chromosome
e	0030527	molecular_function	structural constituent of chromatin
e	0031492	molecular_function	nucleosomal DNA binding
e	0031507	biological_process	heterochromatin formation
e	0046982	molecular_function	protein heterodimerization activity
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005694	cellular_component	chromosome
E	0030527	molecular_function	structural constituent of chromatin
E	0031492	molecular_function	nucleosomal DNA binding
E	0031507	biological_process	heterochromatin formation
E	0046982	molecular_function	protein heterodimerization activity
f	0000786	cellular_component	nucleosome
f	0003677	molecular_function	DNA binding
f	0005515	molecular_function	protein binding
f	0005634	cellular_component	nucleus
f	0005694	cellular_component	chromosome
f	0006334	biological_process	nucleosome assembly
f	0030527	molecular_function	structural constituent of chromatin
f	0031507	biological_process	heterochromatin formation
f	0046982	molecular_function	protein heterodimerization activity
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005694	cellular_component	chromosome
F	0006334	biological_process	nucleosome assembly
F	0030527	molecular_function	structural constituent of chromatin
F	0031507	biological_process	heterochromatin formation
F	0046982	molecular_function	protein heterodimerization activity
g	0000786	cellular_component	nucleosome
g	0003677	molecular_function	DNA binding
g	0005634	cellular_component	nucleus
g	0005694	cellular_component	chromosome
g	0030527	molecular_function	structural constituent of chromatin
g	0031507	biological_process	heterochromatin formation
g	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0005634	cellular_component	nucleus
G	0005694	cellular_component	chromosome
G	0030527	molecular_function	structural constituent of chromatin
G	0031507	biological_process	heterochromatin formation
G	0046982	molecular_function	protein heterodimerization activity
h	0000786	cellular_component	nucleosome
h	0002227	biological_process	innate immune response in mucosa
h	0003677	molecular_function	DNA binding
h	0005515	molecular_function	protein binding
h	0005615	cellular_component	extracellular space
h	0005634	cellular_component	nucleus
h	0005694	cellular_component	chromosome
h	0006325	biological_process	chromatin organization
h	0019731	biological_process	antibacterial humoral response
h	0030527	molecular_function	structural constituent of chromatin
h	0031507	biological_process	heterochromatin formation
h	0046982	molecular_function	protein heterodimerization activity
h	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
H	0000786	cellular_component	nucleosome
H	0002227	biological_process	innate immune response in mucosa
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005615	cellular_component	extracellular space
H	0005634	cellular_component	nucleus
H	0005694	cellular_component	chromosome
H	0006325	biological_process	chromatin organization
H	0019731	biological_process	antibacterial humoral response
H	0030527	molecular_function	structural constituent of chromatin
H	0031507	biological_process	heterochromatin formation
H	0046982	molecular_function	protein heterodimerization activity
H	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
k	0005634	cellular_component	nucleus
k	0006355	biological_process	regulation of DNA-templated transcription
k	0016491	molecular_function	oxidoreductase activity
k	0050660	molecular_function	flavin adenine dinucleotide binding
K	0005634	cellular_component	nucleus
K	0006355	biological_process	regulation of DNA-templated transcription
K	0016491	molecular_function	oxidoreductase activity
K	0050660	molecular_function	flavin adenine dinucleotide binding
m	0005634	cellular_component	nucleus
m	0006355	biological_process	regulation of DNA-templated transcription
m	0016491	molecular_function	oxidoreductase activity
m	0050660	molecular_function	flavin adenine dinucleotide binding
M	0005634	cellular_component	nucleus
M	0006355	biological_process	regulation of DNA-templated transcription
M	0016491	molecular_function	oxidoreductase activity
M	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue FAD M 900

Chain	Residue
E	MET4
M	GLY315
M	ARG316
M	VAL317
M	GLY330
M	ALA331
M	VAL333
M	VAL590
M	THR624
M	LEU625
M	PRO626
M	GLY285
M	LEU659
M	TRP756
M	SER760
M	TYR761
M	GLY800
M	GLU801
M	THR810
M	VAL811
M	ALA814
M	GLY287
M	VAL288
M	SER289
M	GLU308
M	ALA309
M	ARG310
M	GLY314

site_id	AC2
Number of Residues	31
Details	binding site for Di-peptide FAD K 900 and ARG K 310

Chain	Residue
K	GLY285
K	GLY287
K	VAL288
K	SER289
K	LEU307
K	GLU308
K	ALA309
K	ASP311
K	ARG312
K	GLY314
K	GLY315
K	ARG316
K	GLY330
K	ALA331
K	MET332
K	VAL333
K	VAL334
K	LEU586
K	ASN587
K	THR624
K	LEU625
K	ASP754
K	TRP756
K	SER760
K	TYR761
K	GLY800
K	GLU801
K	ALA809
K	THR810
K	VAL811
K	ALA814

site_id	AC3
Number of Residues	29
Details	binding site for Di-peptide FAD K 900 and GLY K 315

Chain	Residue
K	GLY285
K	GLY287
K	VAL288
K	SER289
K	LEU307
K	GLU308
K	ALA309
K	ARG310
K	ARG312
K	VAL313
K	GLY314
K	ARG316
K	VAL317
K	GLY330
K	ALA331
K	MET332
K	VAL333
K	VAL334
K	THR624
K	LEU625
K	TRP756
K	SER760
K	TYR761
K	GLY800
K	GLU801
K	ALA809
K	THR810
K	VAL811
K	ALA814

site_id	AC4
Number of Residues	29
Details	binding site for Di-peptide FAD K 900 and GLY K 330

Chain	Residue
K	ASP328
K	LEU329
K	ALA331
K	MET332
K	VAL333
K	VAL334
K	THR624
K	LEU625
K	TRP751
K	TRP756
K	SER760
K	TYR761
K	GLY800
K	GLU801
K	ALA809
K	THR810
K	VAL811
K	ALA814
K	GLY285
K	GLY287
K	VAL288
K	SER289
K	LEU307
K	GLU308
K	ALA309
K	ARG310
K	GLY314
K	GLY315
K	ARG316

site_id	AC5
Number of Residues	28
Details	binding site for Di-peptide FAD K 900 and VAL K 333

Chain	Residue
K	GLY285
K	GLY287
K	VAL288
K	SER289
K	LEU307
K	GLU308
K	ALA309
K	ARG310
K	GLY314
K	GLY315
K	ARG316
K	GLY330
K	ALA331
K	MET332
K	VAL334
K	LEU565
K	THR566
K	THR624
K	LEU625
K	TRP756
K	SER760
K	TYR761
K	GLY800
K	GLU801
K	ALA809
K	THR810
K	VAL811
K	ALA814

site_id	AC6
Number of Residues	29
Details	binding site for Di-peptide FAD k 900 and ALA k 331

Chain	Residue
k	GLY285
k	SER286
k	GLY287
k	VAL288
k	SER289
k	GLU308
k	ALA309
k	ARG310
k	GLY314
k	GLY315
k	ARG316
k	GLY330
k	MET332
k	VAL333
k	VAL590
k	THR624
k	LEU625
k	PRO626
k	VAL629
k	LEU659
k	TRP756
k	SER760
k	TYR761
k	GLY800
k	GLU801
k	THR810
k	VAL811
k	HIS812
k	ALA814

site_id	AC7
Number of Residues	31
Details	binding site for Di-peptide FAD k 900 and VAL k 811

Chain	Residue
k	GLY285
k	SER286
k	GLY287
k	VAL288
k	SER289
k	GLU308
k	ALA309
k	ARG310
k	GLY314
k	GLY315
k	ARG316
k	ALA331
k	MET332
k	VAL333
k	TYR571
k	VAL590
k	THR624
k	LEU625
k	PRO626
k	VAL629
k	LEU659
k	TRP756
k	SER760
k	TYR761
k	GLY800
k	GLU801
k	THR810
k	HIS812
k	GLY813
k	ALA814
k	LEU815

site_id	AC8
Number of Residues	34
Details	binding site for Di-peptide FAD k 900 and HIS k 812

Chain	Residue
k	GLY285
k	SER286
k	GLY287
k	VAL288
k	SER289
k	GLU308
k	ALA309
k	ARG310
k	GLY314
k	GLY315
k	ARG316
k	ALA331
k	MET332
k	VAL333
k	THR335
k	ASN340
k	MET342
k	VAL590
k	THR624
k	LEU625
k	PRO626
k	VAL629
k	LEU659
k	TRP756
k	SER760
k	TYR761
k	GLY800
k	GLU801
k	THR810
k	VAL811
k	GLY813
k	ALA814
k	LEU815
k	LEU816

site_id	AC9
Number of Residues	33
Details	binding site for Di-peptide FAD k 900 and ALA k 814

Chain	Residue
k	GLY285
k	SER286
k	GLY287
k	VAL288
k	SER289
k	GLU308
k	ALA309
k	ARG310
k	GLY314
k	GLY315
k	ARG316
k	ALA331
k	MET332
k	VAL333
k	VAL590
k	THR624
k	LEU625
k	PRO626
k	VAL629
k	LEU659
k	TRP756
k	SER760
k	TYR761
k	GLY800
k	GLU801
k	THR810
k	VAL811
k	HIS812
k	GLY813
k	LEU815
k	LEU816
k	SER817
k	GLY818

site_id	AD1
Number of Residues	29
Details	binding site for Di-peptide FAD m 900 and GLY m 330

Chain	Residue
m	GLY285
m	SER286
m	GLY287
m	VAL288
m	SER289
m	GLU308
m	ALA309
m	ARG310
m	GLY314
m	GLY315
m	ARG316
m	VAL317
m	ALA318
m	ASP328
m	LEU329
m	ALA331
m	VAL333
m	VAL590
m	THR624
m	LEU625
m	PRO626
m	LYS661
m	TRP751
m	TRP756
m	GLY800
m	GLU801
m	THR810
m	VAL811
m	ALA814

Functional Information from PROSITE/UniProt

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
C	ALA21-VAL27

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY14-HIS18

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
A	LYS14-LEU20

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
D	ARG89-GLY111

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine; by HASPIN and VRK1","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"12138181","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"5-glutamyl serotonin; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"12138181","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Citrulline; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	8
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	4
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	8
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	4
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	4
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	4
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	396
Details	Domain: {"description":"SWIRM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00247","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	484
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16885027","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16956976","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21300290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23721412","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HKO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IW5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2V1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2X0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XAF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XAG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XAH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XAJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XAQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZMU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZMV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZN1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"27292636","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25018020","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	204
Details	Domain: {"description":"SANT 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00624","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)