Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6X0N

Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin

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
O	0000785	cellular_component	chromatin
O	0003682	molecular_function	chromatin binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005694	cellular_component	chromosome
O	0006281	biological_process	DNA repair
O	0006302	biological_process	double-strand break repair
O	0006974	biological_process	DNA damage response
O	0010835	biological_process	regulation of protein ADP-ribosylation
O	0042393	molecular_function	histone binding
O	0072572	molecular_function	poly-ADP-D-ribose binding
O	0090734	cellular_component	site of DNA damage
O	0140768	molecular_function	protein ADP-ribosyltransferase-substrate adaptor activity
O	0140861	biological_process	DNA repair-dependent chromatin remodeling
P	0003677	molecular_function	DNA binding
P	0003682	molecular_function	chromatin binding
P	0003684	molecular_function	damaged DNA binding
P	0003824	molecular_function	catalytic activity
P	0003950	molecular_function	NAD+ poly-ADP-ribosyltransferase activity
P	0005515	molecular_function	protein binding
P	0005634	cellular_component	nucleus
P	0005654	cellular_component	nucleoplasm
P	0005694	cellular_component	chromosome
P	0005730	cellular_component	nucleolus
P	0006281	biological_process	DNA repair
P	0006302	biological_process	double-strand break repair
P	0006974	biological_process	DNA damage response
P	0016740	molecular_function	transferase activity
P	0016757	molecular_function	glycosyltransferase activity
P	0016779	molecular_function	nucleotidyltransferase activity
P	0030592	biological_process	DNA ADP-ribosylation
P	0031491	molecular_function	nucleosome binding
P	0046697	biological_process	decidualization
P	0070212	biological_process	protein poly-ADP-ribosylation
P	0070213	biological_process	protein auto-ADP-ribosylation
P	0072572	molecular_function	poly-ADP-D-ribose binding
P	0090734	cellular_component	site of DNA damage
P	0140294	molecular_function	NAD DNA ADP-ribosyltransferase activity
P	0140805	molecular_function	NAD+-protein-serine ADP-ribosyltransferase activity
P	0140806	molecular_function	NAD+-protein-aspartate ADP-ribosyltransferase activity
P	0140807	molecular_function	NAD+-protein-glutamate ADP-ribosyltransferase activity
P	0140861	biological_process	DNA repair-dependent chromatin remodeling
P	0160004	molecular_function	poly-ADP-D-ribose modification-dependent protein binding
P	1990404	molecular_function	NAD+-protein mono-ADP-ribosyltransferase activity
R	0003677	molecular_function	DNA binding
R	0003682	molecular_function	chromatin binding
R	0003684	molecular_function	damaged DNA binding
R	0003824	molecular_function	catalytic activity
R	0003950	molecular_function	NAD+ poly-ADP-ribosyltransferase activity
R	0005515	molecular_function	protein binding
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005694	cellular_component	chromosome
R	0005730	cellular_component	nucleolus
R	0006281	biological_process	DNA repair
R	0006302	biological_process	double-strand break repair
R	0006974	biological_process	DNA damage response
R	0016740	molecular_function	transferase activity
R	0016757	molecular_function	glycosyltransferase activity
R	0016779	molecular_function	nucleotidyltransferase activity
R	0030592	biological_process	DNA ADP-ribosylation
R	0031491	molecular_function	nucleosome binding
R	0046697	biological_process	decidualization
R	0070212	biological_process	protein poly-ADP-ribosylation
R	0070213	biological_process	protein auto-ADP-ribosylation
R	0072572	molecular_function	poly-ADP-D-ribose binding
R	0090734	cellular_component	site of DNA damage
R	0140294	molecular_function	NAD DNA ADP-ribosyltransferase activity
R	0140805	molecular_function	NAD+-protein-serine ADP-ribosyltransferase activity
R	0140806	molecular_function	NAD+-protein-aspartate ADP-ribosyltransferase activity
R	0140807	molecular_function	NAD+-protein-glutamate ADP-ribosyltransferase activity
R	0140861	biological_process	DNA repair-dependent chromatin remodeling
R	0160004	molecular_function	poly-ADP-D-ribose modification-dependent protein binding
R	1990404	molecular_function	NAD+-protein mono-ADP-ribosyltransferase activity

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	PS00867
Number of Residues	8
Details	CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANPKA

Chain	Residue	Details
P	LEU485-ALA492

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

Chain	Residue	Details
A	PRO66-ILE74

site_id	PS01121
Number of Residues	15
Details	CASPASE_HIS Caspase family histidine active site. HgsrmSnwVgILSHG

Chain	Residue	Details
P	HIS415-GLY429

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
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_FI10
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_FI11
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_FI12
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_FI13
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_FI14
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
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_FI17
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_FI18
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_FI19
Number of Residues	3
Details	Modified residue: {"description":"N6-benzoyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	3
Details	Modified residue: {"description":"N6-isonicotinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	4
Details	Modified residue: {"description":"N6-benzoyllysine; alternate","evidences":[{"source":"UniProtKB","id":"C0HKE1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
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_FI23
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_FI24
Number of Residues	4
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	11
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_FI27
Number of Residues	8
Details	Modified residue: {"description":"N6-isonicotinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q93079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	12
Details	Modified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q93079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
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_FI30
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_FI31
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33683197","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	1
Details	Modified residue: {"description":"PolyADP-ribosyl aspartic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosyltyrosine","evidences":[{"source":"PubMed","id":"29954836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30257210","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	1
Details	Modified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"PubMed","id":"33589610","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	194
Details	Domain: {"description":"WGR","evidences":[{"source":"PROSITE-ProRule","id":"PRU01321","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	117
Details	Domain: {"description":"PARP alpha-helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00398","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	227
Details	Domain: {"description":"PARP catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00397","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	1
Details	Active site: {"description":"For poly [ADP-ribose] polymerase activity","evidences":[{"source":"PubMed","id":"26704974","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30104678","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32028527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6TX3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	1
Details	Site: {"description":"Cleavage; by caspase-8","evidences":[{"source":"UniProtKB","id":"O88554","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)