1O90

Methionine Adenosyltransferase complexed with a L-methionine analogue

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004478	molecular_function	methionine adenosyltransferase activity
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006556	biological_process	S-adenosylmethionine biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0009087	biological_process	methionine catabolic process
A	0016363	cellular_component	nuclear matrix
A	0016597	molecular_function	amino acid binding
A	0016740	molecular_function	transferase activity
A	0042802	molecular_function	identical protein binding
A	0043531	molecular_function	ADP binding
A	0046872	molecular_function	metal ion binding
A	0048269	cellular_component	methionine adenosyltransferase complex
A	0051289	biological_process	protein homotetramerization
A	0065003	biological_process	protein-containing complex assembly
B	0000287	molecular_function	magnesium ion binding
B	0004478	molecular_function	methionine adenosyltransferase activity
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0006556	biological_process	S-adenosylmethionine biosynthetic process
B	0006730	biological_process	one-carbon metabolic process
B	0009087	biological_process	methionine catabolic process
B	0016363	cellular_component	nuclear matrix
B	0016597	molecular_function	amino acid binding
B	0016740	molecular_function	transferase activity
B	0042802	molecular_function	identical protein binding
B	0043531	molecular_function	ADP binding
B	0046872	molecular_function	metal ion binding
B	0048269	cellular_component	methionine adenosyltransferase complex
B	0051289	biological_process	protein homotetramerization
B	0065003	biological_process	protein-containing complex assembly

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A1398

Chain	Residue
A	HIS30
A	LYS266
A	MG1403
B	PO41399

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A1400

Chain	Residue
A	MG1401
B	ASP135
B	ILE323
A	LYS182
A	VAL205
A	SER207
A	PRO247
A	SER248

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A1401

Chain	Residue
A	SER248
A	PO41400
B	ASP135
B	ILE323

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A1402

Chain	Residue
A	ASP180
A	LIS1397

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A1403

Chain	Residue
A	GLU24
A	LYS266
A	PO41398

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A1404

Chain	Residue
A	GLY264
A	ILE267
B	ARG265

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B1399

Chain	Residue
A	ARG265
A	LYS266
A	PO41398
B	GLY280
B	GLY281
B	ALA282
B	LYS286
B	K1405
B	HOH2084

---

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE K B1405

Chain	Residue
B	PO41399

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LIS A1397

Chain	Residue
A	ARG250
A	PHE251
A	MG1402

---

Functional Information from PROSITE/UniProt

site_id	PS00376
Number of Residues	11
Details	ADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY

Chain	Residue	Details
A	GLY132-TYR142

---

site_id	PS00377
Number of Residues	9
Details	ADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD

Chain	Residue	Details
A	GLY279-ASP287

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:1O92, ECO:0007744|PDB:1O9T

Chain	Residue	Details
A	GLU24
B	GLU24

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|PubMed:12888348, ECO:0007744|PDB:1O92, ECO:0007744|PDB:1O93, ECO:0007744|PDB:1O9T

Chain	Residue	Details
A	HIS30
B	HIS30

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P0A817

Chain	Residue	Details
A	GLU58
A	ASP259
B	GLU58
B	ASP259

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: in other chain => ECO:0000250|UniProtKB:P0A817

Chain	Residue	Details
A	GLU71
A	GLN114
A	LYS290
B	GLU71
B	GLN114
B	LYS290

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|PubMed:12888348, ECO:0007744|PDB:1O92, ECO:0007744|PDB:1O9T

Chain	Residue	Details
A	ASP180
B	ASP180

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: in other chain => ECO:0000305|PubMed:10873471, ECO:0000305|PubMed:12888348, ECO:0007744|PDB:1QM4

Chain	Residue	Details
A	SER248
B	SER248

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|PubMed:12888348, ECO:0007744|PDB:1O9T

Chain	Residue	Details
A	ARG265
B	ARG265

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0007744|PDB:1O92

Chain	Residue	Details
A	ALA282
B	ALA282

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12888348, ECO:0007744|PDB:1O92, ECO:0007744|PDB:1O9T

Chain	Residue	Details
A	LYS286
B	LYS286

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:10358060

Chain	Residue	Details
A	CYS121
B	CYS121

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS266
A	HIS30
A	LYS182
A	ARG265
B	LYS286
B	ASP292
B	LYS290

---

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

Chain	Residue	Details
A	LYS286
A	ASP292
A	LYS290
B	LYS266
B	HIS30
B	LYS182
B	ARG265

---