Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KY5

D244E mutant S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001666	biological_process	response to hypoxia
A	0002439	biological_process	chronic inflammatory response to antigenic stimulus
A	0004013	molecular_function	adenosylhomocysteinase activity
A	0005507	molecular_function	copper ion binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006575	biological_process	modified amino acid metabolic process
A	0006730	biological_process	one-carbon metabolic process
A	0006790	biological_process	sulfur compound metabolic process
A	0007584	biological_process	response to nutrient
A	0016787	molecular_function	hydrolase activity
A	0019510	biological_process	S-adenosylhomocysteine catabolic process
A	0030554	molecular_function	adenyl nucleotide binding
A	0033353	biological_process	S-adenosylmethionine cycle
A	0033528	biological_process	S-methylmethionine cycle
A	0042470	cellular_component	melanosome
A	0042745	biological_process	circadian sleep/wake cycle
A	0042802	molecular_function	identical protein binding
A	0051287	molecular_function	NAD binding
A	0098604	molecular_function	adenosylselenohomocysteinase activity
B	0001666	biological_process	response to hypoxia
B	0002439	biological_process	chronic inflammatory response to antigenic stimulus
B	0004013	molecular_function	adenosylhomocysteinase activity
B	0005507	molecular_function	copper ion binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0006575	biological_process	modified amino acid metabolic process
B	0006730	biological_process	one-carbon metabolic process
B	0006790	biological_process	sulfur compound metabolic process
B	0007584	biological_process	response to nutrient
B	0016787	molecular_function	hydrolase activity
B	0019510	biological_process	S-adenosylhomocysteine catabolic process
B	0030554	molecular_function	adenyl nucleotide binding
B	0033353	biological_process	S-adenosylmethionine cycle
B	0033528	biological_process	S-methylmethionine cycle
B	0042470	cellular_component	melanosome
B	0042745	biological_process	circadian sleep/wake cycle
B	0042802	molecular_function	identical protein binding
B	0051287	molecular_function	NAD binding
B	0098604	molecular_function	adenosylselenohomocysteinase activity
C	0001666	biological_process	response to hypoxia
C	0002439	biological_process	chronic inflammatory response to antigenic stimulus
C	0004013	molecular_function	adenosylhomocysteinase activity
C	0005507	molecular_function	copper ion binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0006575	biological_process	modified amino acid metabolic process
C	0006730	biological_process	one-carbon metabolic process
C	0006790	biological_process	sulfur compound metabolic process
C	0007584	biological_process	response to nutrient
C	0016787	molecular_function	hydrolase activity
C	0019510	biological_process	S-adenosylhomocysteine catabolic process
C	0030554	molecular_function	adenyl nucleotide binding
C	0033353	biological_process	S-adenosylmethionine cycle
C	0033528	biological_process	S-methylmethionine cycle
C	0042470	cellular_component	melanosome
C	0042745	biological_process	circadian sleep/wake cycle
C	0042802	molecular_function	identical protein binding
C	0051287	molecular_function	NAD binding
C	0098604	molecular_function	adenosylselenohomocysteinase activity
D	0001666	biological_process	response to hypoxia
D	0002439	biological_process	chronic inflammatory response to antigenic stimulus
D	0004013	molecular_function	adenosylhomocysteinase activity
D	0005507	molecular_function	copper ion binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005829	cellular_component	cytosol
D	0006575	biological_process	modified amino acid metabolic process
D	0006730	biological_process	one-carbon metabolic process
D	0006790	biological_process	sulfur compound metabolic process
D	0007584	biological_process	response to nutrient
D	0016787	molecular_function	hydrolase activity
D	0019510	biological_process	S-adenosylhomocysteine catabolic process
D	0030554	molecular_function	adenyl nucleotide binding
D	0033353	biological_process	S-adenosylmethionine cycle
D	0033528	biological_process	S-methylmethionine cycle
D	0042470	cellular_component	melanosome
D	0042745	biological_process	circadian sleep/wake cycle
D	0042802	molecular_function	identical protein binding
D	0051287	molecular_function	NAD binding
D	0098604	molecular_function	adenosylselenohomocysteinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAI A 432

Chain	Residue
A	THR156
A	GLU242
A	ILE243
A	GLU244
A	ASN247
A	THR274
A	THR275
A	ILE280
A	ILE298
A	GLY299
A	HIS300
A	THR157
A	LEU343
A	ASN345
A	HIS352
A	ADY433
B	LYS1425
B	TYR1429
A	THR158
A	ASN190
A	GLY219
A	GLY221
A	ASP222
A	VAL223
A	THR241

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADY A 433

Chain	Residue
A	LEU53
A	HIS54
A	THR56
A	GLU58
A	THR59
A	ASP130
A	GLU155
A	THR156
A	LYS185
A	ASP189
A	HIS300
A	MET350
A	GLY351
A	HIS352
A	MET357
A	PHE361
A	NAI432

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAI B 1432

Chain	Residue
A	LYS425
A	TYR429
B	THR1156
B	THR1157
B	THR1158
B	ASN1190
B	GLY1219
B	GLY1221
B	ASP1222
B	VAL1223
B	THR1241
B	GLU1242
B	ILE1243
B	GLU1244
B	ASN1247
B	THR1274
B	THR1275
B	ILE1280
B	ILE1298
B	GLY1299
B	HIS1300
B	LEU1343
B	ASN1345
B	HIS1352

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADY B 1433

Chain	Residue
B	LEU1053
B	HIS1054
B	THR1056
B	GLU1058
B	THR1059
B	ASP1130
B	GLU1155
B	THR1156
B	LYS1185
B	ASP1189
B	HIS1300
B	MET1350
B	HIS1352
B	MET1357
B	PHE1361

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAI C 2432

Chain	Residue
C	HIS2300
C	LEU2343
C	ASN2345
C	HIS2352
D	LEU3408
D	LYS3425
D	TYR3429
C	THR2156
C	THR2157
C	THR2158
C	ASN2190
C	GLY2219
C	GLY2221
C	ASP2222
C	VAL2223
C	THR2241
C	GLU2242
C	ILE2243
C	GLU2244
C	ASN2247
C	THR2274
C	THR2275
C	ILE2280
C	ILE2298
C	GLY2299

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADY C 2433

Chain	Residue
C	LEU2053
C	HIS2054
C	THR2056
C	GLU2058
C	THR2059
C	ASP2130
C	GLU2155
C	THR2156
C	LYS2185
C	ASP2189
C	HIS2300
C	MET2350
C	HIS2352
C	MET2357
C	PHE2361

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAI D 3432

Chain	Residue
C	LYS2425
C	TYR2429
D	THR3156
D	THR3157
D	THR3158
D	ASN3190
D	GLY3219
D	GLY3221
D	ASP3222
D	VAL3223
D	THR3241
D	GLU3242
D	ILE3243
D	GLU3244
D	ASN3247
D	THR3274
D	THR3275
D	ILE3280
D	ILE3298
D	GLY3299
D	HIS3300
D	LEU3343
D	ASN3345
D	HIS3352

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADY D 3433

Chain	Residue
D	LEU3053
D	HIS3054
D	THR3056
D	GLU3058
D	THR3059
D	ASP3130
D	GLU3155
D	THR3156
D	LYS3185
D	ASP3189
D	HIS3300
D	MET3350
D	HIS3352
D	MET3357
D	PHE3361

Functional Information from PROSITE/UniProt

site_id	PS00738
Number of Residues	15
Details	ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI

Chain	Residue	Details
A	SER77-ILE91

site_id	PS00739
Number of Residues	17
Details	ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A

Chain	Residue	Details
A	GLY212-ALA228

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10913437","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H5L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387078","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10913437","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H5L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387078","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10913437","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B3R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H5L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387078","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10913437","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B3R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H5L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387078","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B3R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KY4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KY5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XWF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H5L","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P23526","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P23526","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50247","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

Chain	Residue	Details
A	HIS54
A	LYS185
A	ASP189
A	HIS300
A	ASP130
A	CYS194
A	ASN190

site_id	CSA2
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

Chain	Residue	Details
B	ASP1189
B	CYS1194
B	ASN1190
B	HIS1300
B	ASP1130
B	LYS1185
B	HIS1054

site_id	CSA3
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

Chain	Residue	Details
C	LYS2185
C	HIS2054
C	ASN2190
C	ASP2130
C	ASP2189
C	HIS2300
C	CYS2194

site_id	CSA4
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

Chain	Residue	Details
D	HIS3054
D	ASN3190
D	ASP3189
D	HIS3300
D	CYS3194
D	ASP3130
D	LYS3185

site_id	MCSA1
Number of Residues	14
Details	M-CSA 90

Chain	Residue	Details
A	HIS54	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
A	CYS194	electrostatic stabiliser, polar/non-polar interaction
A	HIS300	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS352	electrostatic stabiliser
A	SER360	electrostatic stabiliser, hydrogen bond donor
A	GLN364	activator, electrostatic stabiliser
A	SER77	electrostatic stabiliser
A	SER82	electrostatic stabiliser
A	ASP130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
A	GLU155	electrostatic stabiliser, proton acceptor, proton donor
A	ASN180	activator, electrostatic stabiliser
A	LYS185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
A	ASN190	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA2
Number of Residues	14
Details	M-CSA 90

Chain	Residue	Details
B	HIS1054	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
B	CYS1194	electrostatic stabiliser, polar/non-polar interaction
B	HIS1300	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS1352	electrostatic stabiliser
B	SER1360	electrostatic stabiliser, hydrogen bond donor
B	GLN1364	activator, electrostatic stabiliser
B	SER1077	electrostatic stabiliser
B	SER1082	electrostatic stabiliser
B	ASP1130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
B	GLU1155	electrostatic stabiliser, proton acceptor, proton donor
B	ASN1180	activator, electrostatic stabiliser
B	LYS1185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP1189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
B	ASN1190	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	14
Details	M-CSA 90

Chain	Residue	Details
C	HIS2054	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
C	CYS2194	electrostatic stabiliser, polar/non-polar interaction
C	HIS2300	activator, electrostatic stabiliser, hydrogen bond acceptor
C	HIS2352	electrostatic stabiliser
C	SER2360	electrostatic stabiliser, hydrogen bond donor
C	GLN2364	activator, electrostatic stabiliser
C	SER2077	electrostatic stabiliser
C	SER2082	electrostatic stabiliser
C	ASP2130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
C	GLU2155	electrostatic stabiliser, proton acceptor, proton donor
C	ASN2180	activator, electrostatic stabiliser
C	LYS2185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASP2189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
C	ASN2190	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	14
Details	M-CSA 90

Chain	Residue	Details
D	HIS3054	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
D	CYS3194	electrostatic stabiliser, polar/non-polar interaction
D	HIS3300	activator, electrostatic stabiliser, hydrogen bond acceptor
D	HIS3352	electrostatic stabiliser
D	SER3360	electrostatic stabiliser, hydrogen bond donor
D	GLN3364	activator, electrostatic stabiliser
D	SER3077	electrostatic stabiliser
D	SER3082	electrostatic stabiliser
D	ASP3130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
D	GLU3155	electrostatic stabiliser, proton acceptor, proton donor
D	ASN3180	activator, electrostatic stabiliser
D	LYS3185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASP3189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
D	ASN3190	electrostatic stabiliser, hydrogen bond acceptor

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