Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XWF

K185N mutated S-adenosylhomocysteine hydrolase

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	26
Details	BINDING SITE FOR RESIDUE NAD A 432

Chain	Residue
A	THR157
A	ILE243
A	ASP244
A	ASN247
A	THR274
A	THR275
A	GLY276
A	CYS277
A	ILE280
A	ILE298
A	GLY299
A	ASP189
A	HIS300
A	LEU343
A	ASN345
A	HIS352
B	GLN412
B	LYS425
B	TYR429
A	ASN190
A	GLY219
A	GLY221
A	ASP222
A	VAL223
A	THR241
A	GLU242

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ADN A 433

Chain	Residue
A	HIS54
A	THR56
A	GLU58
A	ASP130
A	GLU155
A	ASP189
A	HIS300
A	LEU343
A	LEU346
A	HIS352
A	MET357
A	PHE361

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD B 432

Chain	Residue
A	GLN412
A	LYS425
A	TYR429
B	THR157
B	ASP189
B	ASN190
B	GLY221
B	ASP222
B	VAL223
B	THR241
B	GLU242
B	ILE243
B	ASP244
B	ASN247
B	THR274
B	THR275
B	GLY276
B	CYS277
B	ILE280
B	ILE298
B	GLY299
B	HIS300
B	LEU343
B	ASN345
B	HIS352

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ADN B 433

Chain	Residue
B	LEU53
B	HIS54
B	THR56
B	GLU58
B	THR59
B	ASP130
B	GLU155
B	ASP189
B	HIS300
B	LEU343
B	LEU346
B	HIS352
B	MET357

site_id	AC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD C 432

Chain	Residue
C	HOH438
D	GLN412
D	LYS425
D	TYR429
C	THR157
C	ASP189
C	ASN190
C	GLY219
C	GLY221
C	ASP222
C	VAL223
C	THR241
C	GLU242
C	ILE243
C	ASP244
C	ASN247
C	THR274
C	THR275
C	GLY276
C	CYS277
C	ILE280
C	ILE298
C	GLY299
C	HIS300
C	LEU343
C	ASN345
C	HIS352

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADN C 433

Chain	Residue
C	HIS54
C	THR56
C	GLU58
C	ASP130
C	GLU155
C	ASP189
C	HIS300
C	LEU343
C	LEU346
C	HIS352
C	MET357

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD D 432

Chain	Residue
C	GLN412
C	LYS425
C	TYR429
D	THR157
D	ASP189
D	ASN190
D	GLY219
D	GLY221
D	ASP222
D	VAL223
D	THR241
D	GLU242
D	ILE243
D	ASP244
D	ASN247
D	THR274
D	THR275
D	GLY276
D	CYS277
D	ILE280
D	ILE298
D	GLY299
D	HIS300
D	LEU343
D	ASN345
D	HIS352
D	HOH435

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADN D 433

Chain	Residue
D	HIS54
D	THR56
D	GLU58
D	ASP130
D	GLU155
D	ASP189
D	LEU343
D	LEU346
D	GLY351
D	HIS352
D	MET357

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	ASN185
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	HIS54
B	ASN185
B	ASP189
B	HIS300
B	ASP130
B	CYS194
B	ASN190

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

Chain	Residue	Details
C	HIS54
C	ASN185
C	ASP189
C	HIS300
C	ASP130
C	CYS194
C	ASN190

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

Chain	Residue	Details
D	HIS54
D	ASN185
D	ASP189
D	HIS300
D	ASP130
D	CYS194
D	ASN190

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	ASN185	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	HIS54	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
B	CYS194	electrostatic stabiliser, polar/non-polar interaction
B	HIS300	activator, electrostatic stabiliser, hydrogen bond acceptor
B	HIS352	electrostatic stabiliser
B	SER360	electrostatic stabiliser, hydrogen bond donor
B	GLN364	activator, electrostatic stabiliser
B	SER77	electrostatic stabiliser
B	SER82	electrostatic stabiliser
B	ASP130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
B	GLU155	electrostatic stabiliser, proton acceptor, proton donor
B	ASN180	activator, electrostatic stabiliser
B	ASN185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
B	ASN190	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA3
Number of Residues	14
Details	M-CSA 90

Chain	Residue	Details
C	HIS54	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
C	CYS194	electrostatic stabiliser, polar/non-polar interaction
C	HIS300	activator, electrostatic stabiliser, hydrogen bond acceptor
C	HIS352	electrostatic stabiliser
C	SER360	electrostatic stabiliser, hydrogen bond donor
C	GLN364	activator, electrostatic stabiliser
C	SER77	electrostatic stabiliser
C	SER82	electrostatic stabiliser
C	ASP130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
C	GLU155	electrostatic stabiliser, proton acceptor, proton donor
C	ASN180	activator, electrostatic stabiliser
C	ASN185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	ASP189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
C	ASN190	electrostatic stabiliser, hydrogen bond acceptor

site_id	MCSA4
Number of Residues	14
Details	M-CSA 90

Chain	Residue	Details
D	HIS54	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
D	CYS194	electrostatic stabiliser, polar/non-polar interaction
D	HIS300	activator, electrostatic stabiliser, hydrogen bond acceptor
D	HIS352	electrostatic stabiliser
D	SER360	electrostatic stabiliser, hydrogen bond donor
D	GLN364	activator, electrostatic stabiliser
D	SER77	electrostatic stabiliser
D	SER82	electrostatic stabiliser
D	ASP130	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
D	GLU155	electrostatic stabiliser, proton acceptor, proton donor
D	ASN180	activator, electrostatic stabiliser
D	ASN185	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	ASP189	electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor
D	ASN190	electrostatic stabiliser, hydrogen bond acceptor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)