Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ENY

Structure of the human PLC editing module

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000139	cellular_component	Golgi membrane
B	0002376	biological_process	immune system process
B	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
B	0002477	biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class Ib
B	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
B	0002503	biological_process	peptide antigen assembly with MHC class II protein complex
B	0002715	biological_process	regulation of natural killer cell mediated immunity
B	0002726	biological_process	positive regulation of T cell cytokine production
B	0005198	molecular_function	structural molecule activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005765	cellular_component	lysosomal membrane
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005794	cellular_component	Golgi apparatus
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0006879	biological_process	intracellular iron ion homeostasis
B	0006955	biological_process	immune response
B	0007608	biological_process	sensory perception of smell
B	0007611	biological_process	learning or memory
B	0009897	cellular_component	external side of plasma membrane
B	0009986	cellular_component	cell surface
B	0010038	biological_process	response to metal ion
B	0012507	cellular_component	ER to Golgi transport vesicle membrane
B	0016020	cellular_component	membrane
B	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
B	0019886	biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II
B	0023026	molecular_function	MHC class II protein complex binding
B	0030670	cellular_component	phagocytic vesicle membrane
B	0031901	cellular_component	early endosome membrane
B	0031902	cellular_component	late endosome membrane
B	0031905	cellular_component	early endosome lumen
B	0033572	biological_process	transferrin transport
B	0034756	biological_process	regulation of iron ion transport
B	0034757	biological_process	negative regulation of iron ion transport
B	0035580	cellular_component	specific granule lumen
B	0042605	molecular_function	peptide antigen binding
B	0042612	cellular_component	MHC class I protein complex
B	0042613	cellular_component	MHC class II protein complex
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0042824	cellular_component	MHC class I peptide loading complex
B	0048260	biological_process	positive regulation of receptor-mediated endocytosis
B	0048261	biological_process	negative regulation of receptor-mediated endocytosis
B	0050680	biological_process	negative regulation of epithelial cell proliferation
B	0050768	biological_process	negative regulation of neurogenesis
B	0050778	biological_process	positive regulation of immune response
B	0050870	biological_process	positive regulation of T cell activation
B	0051289	biological_process	protein homotetramerization
B	0055038	cellular_component	recycling endosome membrane
B	0070062	cellular_component	extracellular exosome
B	0071281	biological_process	cellular response to iron ion
B	0071316	biological_process	cellular response to nicotine
B	1904724	cellular_component	tertiary granule lumen
B	1990000	biological_process	amyloid fibril formation
B	1990712	cellular_component	HFE-transferrin receptor complex
B	2000774	biological_process	positive regulation of cellular senescence
B	2000978	biological_process	negative regulation of forebrain neuron differentiation
C	0000139	cellular_component	Golgi membrane
C	0002398	biological_process	MHC class Ib protein complex assembly
C	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
C	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
C	0005515	molecular_function	protein binding
C	0005783	cellular_component	endoplasmic reticulum
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006457	biological_process	protein folding
C	0006890	biological_process	retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
C	0010468	biological_process	regulation of gene expression
C	0016020	cellular_component	membrane
C	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
C	0023024	molecular_function	MHC class I protein complex binding
C	0030670	cellular_component	phagocytic vesicle membrane
C	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
C	0042288	molecular_function	MHC class I protein binding
C	0042605	molecular_function	peptide antigen binding
C	0042824	cellular_component	MHC class I peptide loading complex
C	0044183	molecular_function	protein folding chaperone
C	0046978	molecular_function	TAP1 binding
C	0046979	molecular_function	TAP2 binding
C	0050823	biological_process	peptide antigen stabilization
C	0051082	molecular_function	unfolded protein binding
C	0060090	molecular_function	molecular adaptor activity
C	0061635	biological_process	regulation of protein complex stability
C	0062061	molecular_function	TAP complex binding
C	0065003	biological_process	protein-containing complex assembly
C	0098553	cellular_component	lumenal side of endoplasmic reticulum membrane
D	0002250	biological_process	adaptive immune response
D	0002376	biological_process	immune system process
D	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
D	0003723	molecular_function	RNA binding
D	0003756	molecular_function	protein disulfide isomerase activity
D	0004197	molecular_function	cysteine-type endopeptidase activity
D	0004629	molecular_function	phospholipase C activity
D	0005515	molecular_function	protein binding
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005783	cellular_component	endoplasmic reticulum
D	0005788	cellular_component	endoplasmic reticulum lumen
D	0005925	cellular_component	focal adhesion
D	0006457	biological_process	protein folding
D	0009986	cellular_component	cell surface
D	0015035	molecular_function	protein-disulfide reductase activity
D	0015036	molecular_function	disulfide oxidoreductase activity
D	0016853	molecular_function	isomerase activity
D	0034975	biological_process	protein folding in endoplasmic reticulum
D	0034976	biological_process	response to endoplasmic reticulum stress
D	0042470	cellular_component	melanosome
D	0042802	molecular_function	identical protein binding
D	0042824	cellular_component	MHC class I peptide loading complex
D	0044183	molecular_function	protein folding chaperone
D	0045335	cellular_component	phagocytic vesicle
D	0055038	cellular_component	recycling endosome membrane
D	0070062	cellular_component	extracellular exosome
D	0106222	molecular_function	lncRNA binding
F	0000139	cellular_component	Golgi membrane
F	0001913	biological_process	T cell mediated cytotoxicity
F	0001916	biological_process	positive regulation of T cell mediated cytotoxicity
F	0002250	biological_process	adaptive immune response
F	0002376	biological_process	immune system process
F	0002419	biological_process	T cell mediated cytotoxicity directed against tumor cell target
F	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
F	0002476	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class Ib
F	0002477	biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class Ib
F	0002485	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent
F	0002486	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent
F	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
F	0002715	biological_process	regulation of natural killer cell mediated immunity
F	0002726	biological_process	positive regulation of T cell cytokine production
F	0003723	molecular_function	RNA binding
F	0005102	molecular_function	signaling receptor binding
F	0005515	molecular_function	protein binding
F	0005615	cellular_component	extracellular space
F	0005783	cellular_component	endoplasmic reticulum
F	0005789	cellular_component	endoplasmic reticulum membrane
F	0005794	cellular_component	Golgi apparatus
F	0005797	cellular_component	Golgi medial cisterna
F	0005886	cellular_component	plasma membrane
F	0006955	biological_process	immune response
F	0009897	cellular_component	external side of plasma membrane
F	0009986	cellular_component	cell surface
F	0012507	cellular_component	ER to Golgi transport vesicle membrane
F	0016020	cellular_component	membrane
F	0016045	biological_process	detection of bacterium
F	0019731	biological_process	antibacterial humoral response
F	0019882	biological_process	antigen processing and presentation
F	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
F	0030670	cellular_component	phagocytic vesicle membrane
F	0030881	molecular_function	beta-2-microglobulin binding
F	0031901	cellular_component	early endosome membrane
F	0032729	biological_process	positive regulation of type II interferon production
F	0036037	biological_process	CD8-positive, alpha-beta T cell activation
F	0042270	biological_process	protection from natural killer cell mediated cytotoxicity
F	0042590	biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I
F	0042605	molecular_function	peptide antigen binding
F	0042608	molecular_function	T cell receptor binding
F	0042610	molecular_function	CD8 receptor binding
F	0042612	cellular_component	MHC class I protein complex
F	0042802	molecular_function	identical protein binding
F	0042824	cellular_component	MHC class I peptide loading complex
F	0045087	biological_process	innate immune response
F	0046977	molecular_function	TAP binding
F	0050830	biological_process	defense response to Gram-positive bacterium
F	0050852	biological_process	T cell receptor signaling pathway
F	0055038	cellular_component	recycling endosome membrane
F	0062061	molecular_function	TAP complex binding
F	0070062	cellular_component	extracellular exosome
F	0070971	cellular_component	endoplasmic reticulum exit site
F	0098553	cellular_component	lumenal side of endoplasmic reticulum membrane
F	2000566	biological_process	positive regulation of CD8-positive, alpha-beta T cell proliferation
F	2000568	biological_process	positive regulation of memory T cell activation
F	2001187	biological_process	positive regulation of CD8-positive, alpha-beta T cell activation
G	0000122	biological_process	negative regulation of transcription by RNA polymerase II
G	0001669	cellular_component	acrosomal vesicle
G	0001849	molecular_function	complement component C1q complex binding
G	0002502	biological_process	peptide antigen assembly with MHC class I protein complex
G	0003677	molecular_function	DNA binding
G	0003723	molecular_function	RNA binding
G	0003729	molecular_function	mRNA binding
G	0005049	molecular_function	nuclear export signal receptor activity
G	0005178	molecular_function	integrin binding
G	0005506	molecular_function	iron ion binding
G	0005509	molecular_function	calcium ion binding
G	0005515	molecular_function	protein binding
G	0005576	cellular_component	extracellular region
G	0005615	cellular_component	extracellular space
G	0005634	cellular_component	nucleus
G	0005635	cellular_component	nuclear envelope
G	0005737	cellular_component	cytoplasm
G	0005739	cellular_component	mitochondrion
G	0005783	cellular_component	endoplasmic reticulum
G	0005788	cellular_component	endoplasmic reticulum lumen
G	0005789	cellular_component	endoplasmic reticulum membrane
G	0005790	cellular_component	smooth endoplasmic reticulum
G	0005829	cellular_component	cytosol
G	0005840	cellular_component	ribosome
G	0005925	cellular_component	focal adhesion
G	0006355	biological_process	regulation of DNA-templated transcription
G	0006457	biological_process	protein folding
G	0006611	biological_process	protein export from nucleus
G	0006874	biological_process	intracellular calcium ion homeostasis
G	0007283	biological_process	spermatogenesis
G	0008270	molecular_function	zinc ion binding
G	0008284	biological_process	positive regulation of cell population proliferation
G	0009410	biological_process	response to xenobiotic stimulus
G	0009897	cellular_component	external side of plasma membrane
G	0009986	cellular_component	cell surface
G	0010595	biological_process	positive regulation of endothelial cell migration
G	0010628	biological_process	positive regulation of gene expression
G	0012505	cellular_component	endomembrane system
G	0016020	cellular_component	membrane
G	0016529	cellular_component	sarcoplasmic reticulum
G	0017148	biological_process	negative regulation of translation
G	0030246	molecular_function	carbohydrate binding
G	0030670	cellular_component	phagocytic vesicle membrane
G	0031012	cellular_component	extracellular matrix
G	0031410	cellular_component	cytoplasmic vesicle
G	0031625	molecular_function	ubiquitin protein ligase binding
G	0032355	biological_process	response to estradiol
G	0032991	cellular_component	protein-containing complex
G	0033018	cellular_component	sarcoplasmic reticulum lumen
G	0033116	cellular_component	endoplasmic reticulum-Golgi intermediate compartment membrane
G	0033144	biological_process	negative regulation of intracellular steroid hormone receptor signaling pathway
G	0033574	biological_process	response to testosterone
G	0034504	biological_process	protein localization to nucleus
G	0034975	biological_process	protein folding in endoplasmic reticulum
G	0036503	biological_process	ERAD pathway
G	0042277	molecular_function	peptide binding
G	0042562	molecular_function	hormone binding
G	0042824	cellular_component	MHC class I peptide loading complex
G	0042921	biological_process	nuclear receptor-mediated glucocorticoid signaling pathway
G	0042981	biological_process	regulation of apoptotic process
G	0044183	molecular_function	protein folding chaperone
G	0044194	cellular_component	cytolytic granule
G	0044322	cellular_component	endoplasmic reticulum quality control compartment
G	0045665	biological_process	negative regulation of neuron differentiation
G	0045787	biological_process	positive regulation of cell cycle
G	0045892	biological_process	negative regulation of DNA-templated transcription
G	0046872	molecular_function	metal ion binding
G	0048387	biological_process	negative regulation of retinoic acid receptor signaling pathway
G	0048471	cellular_component	perinuclear region of cytoplasm
G	0050681	molecular_function	nuclear androgen receptor binding
G	0050766	biological_process	positive regulation of phagocytosis
G	0050821	biological_process	protein stabilization
G	0051082	molecular_function	unfolded protein binding
G	0051087	molecular_function	protein-folding chaperone binding
G	0051604	biological_process	protein maturation
G	0055007	biological_process	cardiac muscle cell differentiation
G	0060473	cellular_component	cortical granule
G	0070062	cellular_component	extracellular exosome
G	0071257	biological_process	cellular response to electrical stimulus
G	0071285	biological_process	cellular response to lithium ion
G	0071682	cellular_component	endocytic vesicle lumen
G	0090398	biological_process	cellular senescence
G	0098553	cellular_component	lumenal side of endoplasmic reticulum membrane
G	0098586	biological_process	cellular response to virus
G	0098794	cellular_component	postsynapse
G	0098978	cellular_component	glutamatergic synapse
G	0140313	molecular_function	molecular sequestering activity
G	1900026	biological_process	positive regulation of substrate adhesion-dependent cell spreading
G	1901164	biological_process	negative regulation of trophoblast cell migration
G	1901652	biological_process	response to peptide
G	1903416	biological_process	response to glycoside
G	1904614	biological_process	response to biphenyl
G	2000510	biological_process	positive regulation of dendritic cell chemotaxis

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. KDEL

Chain	Residue	Details
G	LYS414-LEU417

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LVeFFapWCGHCKrLapeY

Chain	Residue	Details
D	LEU49-TYR67
D	LEU398-TYR416

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH

Chain	Residue	Details
F	TYR257-HIS263
B	TYR78-HIS84

site_id	PS00803
Number of Residues	16
Details	CALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF

Chain	Residue	Details
G	LYS98-PHE113

site_id	PS00804
Number of Residues	9
Details	CALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG

Chain	Residue	Details
G	ILE130-GLY138

site_id	PS00805
Number of Residues	13
Details	CALRETICULIN_REPEAT Calreticulin family repeated motif signature. IkDpDasKPEDWD

Chain	Residue	Details
G	ILE208-ASP220
G	ILE225-ASP237
G	ILE242-ASP254

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	195
Details	Domain: {"description":"Ig-like C1-type"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Pyrrolidone carboxylic acid; in form pI 5.3","evidences":[{"source":"PubMed","id":"7554280","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7918443","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	142
Details	Domain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11825568","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16193070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19119025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35948544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3F8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7QPD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Site: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Site: {"description":"Lowers pKa of C-terminal Cys of first active site","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Site: {"description":"Lowers pKa of C-terminal Cys of second active site","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P27773","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27773","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	86
Details	Domain: {"description":"Ig-like C1-type","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	89
Details	Region: {"description":"Alpha-1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	91
Details	Region: {"description":"Alpha-2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	91
Details	Region: {"description":"Alpha-3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21943705","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21543847","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	11
Details	Repeat: {"description":"1-1"}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	11
Details	Repeat: {"description":"1-2"}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	11
Details	Repeat: {"description":"1-3"}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	11
Details	Repeat: {"description":"1-4"}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	10
Details	Repeat: {"description":"2-1"}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	10
Details	Repeat: {"description":"2-3"}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	179
Details	Region: {"description":"N-domain"}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	33
Details	Region: {"description":"Interaction with PPIB","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	9
Details	Compositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	27
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21423620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27840680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3POS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3POW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LK5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14211","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	1
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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