5AXB

Crystal structure of mouse SAHH complexed with noraristeromycin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004013	molecular_function	adenosylhomocysteinase activity
A	0005507	molecular_function	copper ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0016787	molecular_function	hydrolase activity
A	0019510	biological_process	S-adenosylhomocysteine catabolic process
A	0042470	cellular_component	melanosome
A	0042802	molecular_function	identical protein binding
A	0051287	molecular_function	NAD binding
C	0004013	molecular_function	adenosylhomocysteinase activity
C	0005507	molecular_function	copper ion binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0006730	biological_process	one-carbon metabolic process
C	0016787	molecular_function	hydrolase activity
C	0019510	biological_process	S-adenosylhomocysteine catabolic process
C	0042470	cellular_component	melanosome
C	0042802	molecular_function	identical protein binding
C	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	binding site for residue NAD A 501

Chain	Residue
A	THR157
A	ILE244
A	ASP245
A	ASN248
A	THR275
A	THR276
A	CYS278
A	ILE281
A	ILE299
A	GLY300
A	HIS301
A	THR158
A	LEU344
A	ASN346
A	HIS353
A	GLN413
A	LYS426
A	TYR430
A	NRN502
A	HOH665
A	HOH718
A	HOH768
A	THR159
A	HOH827
A	HOH861
A	HOH878
A	ASN191
A	GLY222
A	ASP223
A	VAL224
A	THR242
A	GLU243

---

site_id	AC2
Number of Residues	15
Details	binding site for residue NRN A 502

Chain	Residue
A	HIS55
A	THR57
A	GLU59
A	THR60
A	ASP131
A	GLU156
A	THR157
A	LYS186
A	ASP190
A	MET351
A	HIS353
A	MET358
A	PHE362
A	NAD501
A	HOH639

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 503

Chain	Residue
A	GLU59
A	HOH660
A	HOH767
A	HOH1016
C	ASP208
C	HOH658

---

site_id	AC4
Number of Residues	31
Details	binding site for residue NAD C 501

Chain	Residue
C	THR157
C	THR158
C	THR159
C	ASN191
C	GLY222
C	ASP223
C	VAL224
C	THR242
C	GLU243
C	ILE244
C	ASP245
C	ASN248
C	THR275
C	THR276
C	CYS278
C	ILE281
C	ILE299
C	GLY300
C	HIS301
C	ASN346
C	HIS353
C	GLN413
C	LYS426
C	TYR430
C	NRN502
C	HOH657
C	HOH772
C	HOH819
C	HOH833
C	HOH834
C	HOH880

---

site_id	AC5
Number of Residues	15
Details	binding site for residue NRN C 502

Chain	Residue
C	THR57
C	GLU59
C	THR60
C	ASP131
C	GLU156
C	THR157
C	LYS186
C	ASP190
C	MET351
C	HIS353
C	MET358
C	PHE362
C	NAD501
C	HOH660
C	HOH761

---

site_id	AC6
Number of Residues	6
Details	binding site for residue NA C 503

Chain	Residue
A	ASP208
A	HOH688
C	GLU59
C	HOH711
C	HOH723
C	HOH994

---

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	SER78-ILE92

---

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

Chain	Residue	Details
A	GLY213-ALA229

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P10760

Chain	Residue	Details
A	THR57
C	ASP190
A	ASP131
A	GLU156
A	LYS186
A	ASP190
C	THR57
C	ASP131
C	GLU156
C	LYS186

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P23526

Chain	Residue	Details
A	SER2
C	SER2

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23526

Chain	Residue	Details
A	SER183
C	SER183

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P23526

Chain	Residue	Details
A	LYS186
C	LYS186

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	TYR193
C	TYR193

---