3N58

Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004013	molecular_function	adenosylhomocysteinase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0016787	molecular_function	hydrolase activity
A	0033353	biological_process	S-adenosylmethionine cycle
A	0071269	biological_process	L-homocysteine biosynthetic process
B	0004013	molecular_function	adenosylhomocysteinase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006730	biological_process	one-carbon metabolic process
B	0016787	molecular_function	hydrolase activity
B	0033353	biological_process	S-adenosylmethionine cycle
B	0071269	biological_process	L-homocysteine biosynthetic process
C	0004013	molecular_function	adenosylhomocysteinase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006730	biological_process	one-carbon metabolic process
C	0016787	molecular_function	hydrolase activity
C	0033353	biological_process	S-adenosylmethionine cycle
C	0071269	biological_process	L-homocysteine biosynthetic process
D	0004013	molecular_function	adenosylhomocysteinase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006730	biological_process	one-carbon metabolic process
D	0016787	molecular_function	hydrolase activity
D	0033353	biological_process	S-adenosylmethionine cycle
D	0071269	biological_process	L-homocysteine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 2

Chain	Residue
A	GLN59
A	THR385
A	GLY386
A	HIS387
A	HOH521

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADN A 500

Chain	Residue
A	ASP132
A	GLU192
A	THR193
A	LYS222
A	ASP226
A	HIS337
A	LEU378
A	THR385
A	HIS387
A	MET392
A	NAD550
A	HIS55
A	THR57
A	GLN59
A	THR60

---

site_id	AC3
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD A 550

Chain	Residue
A	THR193
A	THR194
A	THR195
A	ASP226
A	ASN227
A	GLY256
A	GLY258
A	ASP259
A	VAL260
A	THR278
A	GLU279
A	VAL280
A	ASP281
A	CYS284
A	THR311
A	THR312
A	GLY313
A	ASN314
A	ILE335
A	GLY336
A	HIS337
A	ASN380
A	HIS387
A	HOH471
A	HOH479
A	HOH492
A	ADN500
A	HOH534
A	HOH577
A	HOH653
B	LYS460
B	TYR464

---

site_id	AC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD B 550

Chain	Residue
A	LYS460
A	TYR464
B	ASN227
B	GLY256
B	GLY258
B	ASP259
B	VAL260
B	THR278
B	GLU279
B	VAL280
B	ASP281
B	CYS284
B	THR311
B	THR312
B	GLY313
B	ASN314
B	ILE335
B	GLY336
B	HIS337
B	ASN380
B	HIS387
B	HOH498
B	HOH523
B	HOH526
B	HOH543

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 1

Chain	Residue
C	GLN59
C	THR385
C	GLY386
C	HIS387
C	HOH479

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADN C 500

Chain	Residue
C	NAD550
C	LEU54
C	HIS55
C	THR57
C	GLN59
C	THR60
C	ASP132
C	GLU192
C	THR193
C	LYS222
C	ASP226
C	HIS337
C	LEU378
C	THR385
C	GLY386
C	HIS387
C	MET392
C	PHE396

---

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD C 550

Chain	Residue
C	THR193
C	THR194
C	THR195
C	ASN227
C	GLY256
C	GLY258
C	ASP259
C	VAL260
C	THR278
C	GLU279
C	VAL280
C	ASP281
C	THR311
C	THR312
C	GLY313
C	ASN314
C	ILE335
C	GLY336
C	HIS337
C	ASN380
C	HIS387
C	HOH473
C	HOH478
C	ADN500
C	HOH512
C	HOH539
C	HOH578
C	HOH579
D	LYS460
D	TYR464

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 467

Chain	Residue
D	GLN59
D	THR385
D	GLY386
D	HIS387

---

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADN D 500

Chain	Residue
D	LEU54
D	HIS55
D	THR57
D	GLN59
D	THR60
D	ASP132
D	GLU192
D	THR193
D	LYS222
D	ASP226
D	HIS337
D	LEU378
D	THR385
D	HIS387
D	MET392
D	PHE396
D	NAD550

---

site_id	BC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAD D 550

Chain	Residue
C	GLN447
C	LYS460
C	TYR464
C	HOH490
D	THR193
D	THR194
D	THR195
D	ASN227
D	GLY256
D	GLY258
D	ASP259
D	VAL260
D	THR278
D	GLU279
D	VAL280
D	ASP281
D	CYS284
D	THR311
D	THR312
D	GLY313
D	ASN314
D	ILE335
D	GLY336
D	HIS337
D	LEU378
D	ASN380
D	HIS387
D	HOH482
D	ADN500
D	HOH511
D	HOH516

---

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. GKvavVcGYGdVGKGs.A

Chain	Residue	Details
A	GLY249-ALA265

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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