dbSNO

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

PDB ID: 4IBM
Chain: B
Site: 1056


	PTM	Style	Surface	Display
SNO: B_1056
Flank: B_1050~1062
Other chain
Other site
All protein
Other Function
Chain		B-factor
Charge		Ligand

	PDB site	Amino Acid	Distance(A)	Secondary Structure	Accessible surface area	Side Chian Angle
-6	1050	V	>10	H	61	-
	1051	M	>10	H	5	-
	1052	K	>10	C	52	-
	1053	G	>10	C	41	-
	1054	F	7.711	C	14	-
	1055	T	6.365	C	101	-
Center	1056	C	-	C	15	-
+6	1057	H	4.5	C	72	-
	1058	H	4.1	C	1	-
	1059	V	5.115	E	2
	1060	V	8.512	C	2	-
	1061	R	9.326	C	27	-
	1062	L	>10	E	7	-
Other site of 17	1119	G	4.2	H	0	-
	1276	F	5	C	8	-
	1122	Y	5.185	H	3
	1118	D	6.087	H	0
	1275	S	6.176	C	5	-
	1123	L	7.456	H	0
	1120	M	7.459	H	0	-
	1121	A	7.634	H	6	-
	1274	V	7.981	H	41	-
	1147	K	8.024	E	10
	1115	E	8.325	H	11	-
	1277	F	8.355	C	37	-
	1148	I	8.386	E	0
	1116	I	8.859	H	0	-
	1117	A	9.209	H	0	-
	1279	S	9.425	C	40
	1281	E	9.883	C	92

Show

Neighbor Amino Acid Top 3
Distance(A)	PDB site	Amino Acid	Secondary Structure	Accessible surface area	Side Chian Angle	Single
4.1	1058	H	C	1
4.2	1119	G	H	0	-
4.5	1057	H	C	72

TOP 3

Amino acid modifications

Amino acid modifications image of Seq Distance (Amino Acid) of Cysteine:

Feature Key	Seq Position	Seq Distance (Amino Acid) of Cysteine	Space Distance(A)	Description
Modified residue	400	-683	Outside Of PDB File	Phosphoserine
Modified residue	401	-682	Outside Of PDB File	Phosphotyrosine
Modified residue	407	-676	Outside Of PDB File	Phosphoserine
Modified residue	999	-84	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1185	102		Phosphotyrosine; by autocatalysis
Modified residue	1189	106		Phosphotyrosine; by autocatalysis
Modified residue	1190	107		Phosphotyrosine; by autocatalysis
Modified residue	1355	272	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1361	278	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Glycosylation	43	-1040	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	52	-1031	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	138	-945	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	242	-841	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	282	-801	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	364	-719	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	424	-659	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	445	-638	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	541	-542	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	769	-314	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	920	-163	Outside Of PDB File	N-linked (GlcNAc...)
Disulfide bond	35<-->53	-1048<-->-1030	Outside Of PDB File
Disulfide bond	153<-->182	-930<-->-901	Outside Of PDB File
Disulfide bond	186<-->209	-897<-->-874	Outside Of PDB File
Disulfide bond	196<-->215	-887<-->-868	Outside Of PDB File
Disulfide bond	219<-->228	-864<-->-855	Outside Of PDB File
Disulfide bond	223<-->234	-860<-->-849	Outside Of PDB File
Disulfide bond	235<-->243	-848<-->-840	Outside Of PDB File
Disulfide bond	239<-->252	-844<-->-831	Outside Of PDB File
Disulfide bond	255<-->264	-828<-->-819	Outside Of PDB File
Disulfide bond	268<-->280	-815<-->-803	Outside Of PDB File
Disulfide bond	286<-->311	-797<-->-772	Outside Of PDB File
Disulfide bond	293<-->301	-790<-->-782	Outside Of PDB File
Disulfide bond	315<-->328	-768<-->-755	Outside Of PDB File
Disulfide bond	331<-->335	-752<-->-748	Outside Of PDB File
Disulfide bond	339<-->360	-744<-->-723	Outside Of PDB File
Disulfide bond	462<-->495	-621<-->-588	Outside Of PDB File
Disulfide bond	551	-532	Outside Of PDB File
Disulfide bond	674<-->899	-409<-->-184	Outside Of PDB File
Disulfide bond	825<-->834	-258<-->-249	Outside Of PDB File

Binding site

Binding site image of Seq Distance (Amino Acid) of Cysteine:

Feature Key	Seq Position	Seq Distance (Amino Acid) of Cysteine	Space Distance(A)	Description
Binding site	1033	-50		ATP
Binding site	1057	-26		ATP
Binding site	1177	94		ATP

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