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: 4KRM
Chain: G
Site: 446


	PTM	Style	Surface	Display
SNO: G_446
Flank: G_440~452
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	440	S	>10	E	17	-
	441	G	>10	C	21	-
	442	N	9.826	C	0	-
	443	K	8.846	C	53	-
	444	N	6.044	C	46	-
	445	L	4.978	C	1	-
Center	446	q	-	C	5	-
+6	447	Y	5.954	C	19
	448	A	8.276	C	5	-
	449	N	9.927	C	109	-
	450	T	>10	C	54	-
	451	I	>10	C	13	-
	452	N	>10	C	93	-
Other site of 19	475	C	3.824	H	6
	480	Q	5.012	C	34
	470	R	5.615	C	81
	422	T	6.005	C	39	-
	472	E	6.636	H	147	-
	474	S	6.746	H	53
	481	V	6.943	C	74	-
	471	G	6.972	C	42	-
	423	S	7.219	C	4	-
	476	K	7.233	H	59	-
	478	T	7.614	C	82
	479	G	8.264	C	54	-
	469	N	8.347	C	32	-
	473	N	8.524	H	141	-
	493	G	9.065	C	0	-
	477	A	9.087	C	92	-
	494	P	9.285	C	51
	421	I	9.409	C	1	-
	482	C	9.831	C	34	-

Show

Neighbor Amino Acid Top 3
Distance(A)	PDB site	Amino Acid	Secondary Structure	Accessible surface area	Side Chian Angle	Single
3.824	475	C	H	6
4.978	445	L	C	1
5.012	480	Q	C	34

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	229	-241	Outside Of PDB File	Phosphoserine
Modified residue	678	208	Outside Of PDB File	Phosphothreonine; by PKC and PKD/PRKD1
Modified residue	693	223	Outside Of PDB File	Phosphothreonine; by PKD/PRKD1
Modified residue	695	225	Outside Of PDB File	Phosphoserine
Modified residue	991	521	Outside Of PDB File	Phosphoserine
Modified residue	995	525	Outside Of PDB File	Phosphoserine
Modified residue	998	528	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1016	546	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1026	556	Outside Of PDB File	Phosphoserine
Modified residue	1039	569	Outside Of PDB File	Phosphoserine
Modified residue	1041	571	Outside Of PDB File	Phosphothreonine
Modified residue	1042	572	Outside Of PDB File	Phosphoserine
Modified residue	1064	594	Outside Of PDB File	Phosphoserine
Modified residue	1070	600	Outside Of PDB File	Phosphoserine
Modified residue	1071	601	Outside Of PDB File	Phosphoserine
Modified residue	1081	611	Outside Of PDB File	Phosphoserine
Modified residue	1092	622	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1110	640	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1166	696	Outside Of PDB File	Phosphoserine
Modified residue	1172	702	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1197	727	Outside Of PDB File	Phosphotyrosine; by autocatalysis
Modified residue	1199	729	Outside Of PDB File	Omega-N-methylated arginine
Glycosylation	56	-414	Outside Of PDB File	N-linked (GlcNAc...) (complex); partial; atypical
Glycosylation	73	-397	Outside Of PDB File	N-linked (GlcNAc...); atypical
Glycosylation	128	-342	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	175	-295	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	196	-274	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	352	-118	Outside Of PDB File	N-linked (GlcNAc...)
Glycosylation	361	-109		N-linked (GlcNAc...)
Glycosylation	413	-57		N-linked (GlcNAc...)
Glycosylation	444	-26		N-linked (GlcNAc...)
Glycosylation	528	58		N-linked (GlcNAc...)
Glycosylation	568	98	Outside Of PDB File	N-linked (GlcNAc...); partial
Glycosylation	603	133	Outside Of PDB File	N-linked (GlcNAc...); partial
Disulfide bond	31<-->58	-439<-->-412	Outside Of PDB File
Disulfide bond	157<-->187	-313<-->-283	Outside Of PDB File
Disulfide bond	190<-->199	-280<-->-271	Outside Of PDB File
Disulfide bond	194<-->207	-276<-->-263	Outside Of PDB File
Disulfide bond	215<-->223	-255<-->-247	Outside Of PDB File
Disulfide bond	219<-->231	-251<-->-239	Outside Of PDB File
Disulfide bond	232<-->240	-238<-->-230	Outside Of PDB File
Disulfide bond	236<-->248	-234<-->-222	Outside Of PDB File
Disulfide bond	251<-->260	-219<-->-210	Outside Of PDB File
Disulfide bond	264<-->291	-206<-->-179	Outside Of PDB File
Disulfide bond	295<-->307	-175<-->-163	Outside Of PDB File
Disulfide bond	311<-->326	-159<-->-144	Outside Of PDB File
Disulfide bond	329<-->333	-141<-->-137	Outside Of PDB File
Disulfide bond	337<-->362	-133<-->-108	<-->
Disulfide bond	470<-->499	0<-->29	<-->
Disulfide bond	506<-->515	36<-->45	<-->
Disulfide bond	510<-->523	40<-->53	<-->
Disulfide bond	526<-->535	56<-->65	<-->
Disulfide bond	539<-->555	69<-->85	Outside Of PDB File
Disulfide bond	558<-->571	88<-->101	Outside Of PDB File
Disulfide bond	562<-->579	92<-->109	Outside Of PDB File
Disulfide bond	582<-->591	112<-->121	Outside Of PDB File
Disulfide bond	595<-->617	125<-->147	Outside Of PDB File
Disulfide bond	620<-->628	150<-->158	Outside Of PDB File
Disulfide bond	624<-->636	154<-->166	Outside Of PDB File
Cross-link	716	246	Outside Of PDB File
Cross-link	737	267	Outside Of PDB File
Cross-link	754	284	Outside Of PDB File
Cross-link	867	397	Outside Of PDB File
Cross-link	929	459	Outside Of PDB File
Cross-link	970	500	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	745	275	Outside Of PDB File	ATP
Binding site	855	385	Outside Of PDB File	ATP

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