1XRA

CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004478	molecular_function	methionine adenosyltransferase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006556	biological_process	S-adenosylmethionine biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0033353	biological_process	S-adenosylmethionine cycle
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 384

Chain	Residue
A	HIS14
A	ASP118
A	LYS165
A	LYS245
A	PO4385
A	MG411
A	MG412

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 385

Chain	Residue
A	LYS245
A	LYS265
A	PO4384
A	MG412
A	ASP16
A	ARG244

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 411

Chain	Residue
A	ASP118
A	ASP271
A	PO4384

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 412

Chain	Residue
A	ASP16
A	PO4384
A	PO4385

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 413

Chain	Residue
A	GLU42
A	ARG244
A	SER263
A	LYS265

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site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K A 414

Chain	Residue
A	GLY243
A	GLY243

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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	GLY115-TYR125

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

Chain	Residue	Details
A	GLY258-ASP266

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9

Chain	Residue	Details
A	HIS14
A	GLU55
A	GLN98
A	ASP163
A	ARG229
A	ARG244
A	LYS269

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9

Chain	Residue	Details
A	ASP16
A	ALA261
A	LYS265

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0000305|PubMed:7629147, ECO:0007744|PDB:1MXC, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9

Chain	Residue	Details
A	GLU42

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L

Chain	Residue	Details
A	ASP238

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS2

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1fug

Chain	Residue	Details
A	LYS269
A	LYS265
A	ASP271

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site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1fug

Chain	Residue	Details
A	LYS245
A	HIS14
A	LYS165
A	ARG244

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