2H5L

S-Adenosylhomocysteine hydrolase containing NAD and 3-deaza-D-eritadenine

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD A 432

Chain	Residue
A	THR156
A	GLU242
A	ILE243
A	ASP244
A	ASN247
A	THR274
A	THR275
A	ILE280
A	ILE298
A	GLY299
A	HIS300
A	THR157
A	LEU343
A	ASN345
A	HIS352
A	3DD433
A	HOH437
A	HOH468
B	GLN412
B	LYS425
B	TYR429
B	HOH441
A	THR158
A	ASN190
A	GLY219
A	GLY221
A	ASP222
A	VAL223
A	THR241

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD 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	LEU346
A	GLY351
A	HIS352
A	PHE361
A	NAD432

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD B 432

Chain	Residue
A	GLN412
A	LYS425
A	TYR429
B	THR156
B	THR157
B	THR158
B	ASN190
B	GLY219
B	GLY221
B	ASP222
B	VAL223
B	THR241
B	GLU242
B	ILE243
B	ASP244
B	ASN247
B	THR274
B	THR275
B	ILE280
B	ILE298
B	GLY299
B	HIS300
B	LEU343
B	ASN345
B	HIS352
B	3DD433

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD B 433

Chain	Residue
B	LEU53
B	HIS54
B	THR56
B	GLU58
B	THR59
B	ASP130
B	GLU155
B	THR156
B	LYS185
B	ASP189
B	LEU346
B	GLY351
B	HIS352
B	PHE361
B	NAD432

---

site_id	AC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD C 432

Chain	Residue
C	THR275
C	ILE280
C	ILE298
C	GLY299
C	HIS300
C	LEU343
C	ASN345
C	HIS352
C	3DD433
D	GLN412
D	LYS425
D	TYR429
C	THR156
C	THR157
C	THR158
C	ASN190
C	GLY219
C	GLY221
C	ASP222
C	VAL223
C	THR241
C	GLU242
C	ILE243
C	ASP244
C	ASN247
C	THR274

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD C 433

Chain	Residue
C	LEU53
C	HIS54
C	THR56
C	GLU58
C	THR59
C	ASP130
C	GLU155
C	THR156
C	LYS185
C	ASP189
C	LEU346
C	GLY351
C	HIS352
C	PHE361
C	NAD432

---

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD D 432

Chain	Residue
C	GLN412
C	LYS425
C	TYR429
D	THR156
D	THR157
D	THR158
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	ILE280
D	ILE298
D	GLY299
D	HIS300
D	LEU343
D	ASN345
D	HIS352
D	3DD433

---

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD D 433

Chain	Residue
D	LEU53
D	HIS54
D	THR56
D	GLU58
D	THR59
D	ASP130
D	GLU155
D	THR156
D	LYS185
D	ASP189
D	LEU346
D	GLY351
D	HIS352
D	PHE361
D	NAD432

---

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD E 432

Chain	Residue
E	THR156
E	THR157
E	THR158
E	ASN190
E	GLY219
E	GLY221
E	ASP222
E	VAL223
E	THR241
E	GLU242
E	ILE243
E	ASP244
E	ASN247
E	THR274
E	THR275
E	ILE280
E	ILE298
E	GLY299
E	HIS300
E	LEU343
E	ASN345
E	HIS352
E	3DD433
E	HOH486
F	GLN412
F	LYS425
F	TYR429

---

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD E 433

Chain	Residue
E	LEU53
E	HIS54
E	THR56
E	GLU58
E	THR59
E	ASP130
E	GLU155
E	THR156
E	LYS185
E	ASP189
E	LEU346
E	GLY351
E	HIS352
E	PHE361
E	NAD432

---

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD F 432

Chain	Residue
E	GLN412
E	LYS425
E	TYR429
F	THR156
F	THR157
F	THR158
F	ASN190
F	GLY219
F	GLY221
F	ASP222
F	VAL223
F	THR241
F	GLU242
F	ILE243
F	ASP244
F	ASN247
F	THR274
F	THR275
F	ILE280
F	ILE298
F	GLY299
F	HIS300
F	LEU343
F	ASN345
F	HIS352
F	3DD433

---

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD F 433

Chain	Residue
F	LEU53
F	HIS54
F	THR56
F	GLU58
F	THR59
F	ASP130
F	GLU155
F	THR156
F	LYS185
F	ASP189
F	LEU346
F	GLY351
F	HIS352
F	PHE361
F	NAD432

---

site_id	BC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD G 432

Chain	Residue
G	THR156
G	THR157
G	THR158
G	ASN190
G	GLY219
G	GLY221
G	ASP222
G	VAL223
G	THR241
G	GLU242
G	ILE243
G	ASP244
G	ASN247
G	THR274
G	THR275
G	ILE280
G	ILE298
G	GLY299
G	HIS300
G	LEU343
G	ASN345
G	HIS352
G	3DD433
H	GLN412
H	LYS425
H	TYR429

---

site_id	BC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD G 433

Chain	Residue
G	LEU53
G	HIS54
G	THR56
G	GLU58
G	THR59
G	ASP130
G	GLU155
G	THR156
G	LYS185
G	ASP189
G	LEU346
G	GLY351
G	HIS352
G	PHE361
G	NAD432

---

site_id	BC6
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD H 432

Chain	Residue
G	GLN412
G	LYS425
G	TYR429
H	THR156
H	THR157
H	THR158
H	ASN190
H	GLY219
H	GLY221
H	ASP222
H	VAL223
H	THR241
H	GLU242
H	ILE243
H	ASP244
H	ASN247
H	THR274
H	THR275
H	ILE280
H	ILE298
H	GLY299
H	HIS300
H	LEU343
H	ASN345
H	HIS352
H	3DD433
H	HOH449

---

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 3DD H 433

Chain	Residue
H	LEU53
H	HIS54
H	THR56
H	GLU58
H	THR59
H	ASP130
H	GLU155
H	THR156
H	LYS185
H	ASP189
H	LEU346
H	GLY351
H	HIS352
H	PHE361
H	NAD432

---

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	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11741948","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11927587","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
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	16
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	80
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10387078","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
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":"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	32
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	8
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	8
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	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P23526","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	8
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	8
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	HIS54
B	LYS185
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	LYS185
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	LYS185
D	ASP189
D	HIS300
D	ASP130
D	CYS194
D	ASN190

---

site_id	CSA5
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

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

---

site_id	CSA6
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

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

---

site_id	CSA7
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

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

---

site_id	CSA8
Number of Residues	7
Details	Annotated By Reference To The Literature 1b3r

Chain	Residue	Details
H	HIS54
H	LYS185
H	ASP189
H	HIS300
H	ASP130
H	CYS194
H	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	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	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	LYS185	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	LYS185	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	LYS185	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

---

site_id	MCSA5
Number of Residues	14
Details	M-CSA 90

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

---

site_id	MCSA6
Number of Residues	14
Details	M-CSA 90

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

---

site_id	MCSA7
Number of Residues	14
Details	M-CSA 90

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

---

site_id	MCSA8
Number of Residues	14
Details	M-CSA 90

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

---