Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6SW5

Crystal structure of the human S-adenosylmethionine synthetase 1 (ligand-free form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004478	molecular_function	methionine adenosyltransferase activity
A	0005515	molecular_function	protein binding
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	0016740	molecular_function	transferase activity
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048269	cellular_component	methionine adenosyltransferase complex
A	0051289	biological_process	protein homotetramerization
B	0004478	molecular_function	methionine adenosyltransferase activity
B	0005515	molecular_function	protein binding
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	0016740	molecular_function	transferase activity
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048269	cellular_component	methionine adenosyltransferase complex
B	0051289	biological_process	protein homotetramerization
C	0004478	molecular_function	methionine adenosyltransferase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006556	biological_process	S-adenosylmethionine biosynthetic process
C	0006730	biological_process	one-carbon metabolic process
C	0009087	biological_process	methionine catabolic process
C	0016740	molecular_function	transferase activity
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048269	cellular_component	methionine adenosyltransferase complex
C	0051289	biological_process	protein homotetramerization
D	0004478	molecular_function	methionine adenosyltransferase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0006556	biological_process	S-adenosylmethionine biosynthetic process
D	0006730	biological_process	one-carbon metabolic process
D	0009087	biological_process	methionine catabolic process
D	0016740	molecular_function	transferase activity
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0048269	cellular_component	methionine adenosyltransferase complex
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue PEG A 401

Chain	Residue
A	GLN317
A	PHE333
B	ARG313
B	PEG1001

site_id	AC2
Number of Residues	8
Details	binding site for residue EDO A 402

Chain	Residue
A	ALA276
B	ALA276
B	HIS277
A	ILE267
A	TYR271
A	GLY273
A	TRP274
A	GLY275

site_id	AC3
Number of Residues	8
Details	binding site for residue EDO A 403

Chain	Residue
A	MET138
A	PHE139
A	THR270
A	HIS277
A	GLY278
A	PHE282
A	HOH531
A	HOH548

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 404

Chain	Residue
A	GLN187
A	ARG199
A	HOH556

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO A 405

Chain	Residue
A	GLU326
A	HIS350
A	PHE353
A	LEU355

site_id	AC6
Number of Residues	3
Details	binding site for residue EDO A 406

Chain	Residue
A	ASP144
A	THR146
A	LYS307

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 407

Chain	Residue
A	GLY275
A	ARG313
A	HOH553
B	PEG1001

site_id	AC8
Number of Residues	7
Details	binding site for residue PEG B 1001

Chain	Residue
A	LEU315
A	TYR335
A	PEG401
A	EDO407
B	GLY275
B	TYR335
B	HOH1147

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO B 1002

Chain	Residue
B	PHE139
B	HIS277
B	GLY278
B	ALA295

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO B 1003

Chain	Residue
B	THR146
B	GLU148
B	LYS159
B	HOH1110

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO C 401

Chain	Residue
C	GLN36
C	HIS89
C	GLN372
C	CYS376

site_id	AD3
Number of Residues	5
Details	binding site for residue EDO C 402

Chain	Residue
C	GLY275
C	ARG313
C	HOH532
C	HOH557
D	LEU315

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO C 403

Chain	Residue
C	GLU148
C	PRO232

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO D 401

Chain	Residue
D	GLU326
D	HIS350
D	PHE353
D	LEU355
D	HOH515

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	GLY131-TYR141

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

Chain	Residue	Details
A	GLY278-ASP286

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P13444

Chain	Residue	Details
A	GLU23
B	GLU23
C	GLU23
D	GLU23

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: in other chain => ECO:0000305\|PubMed:23425511, ECO:0007744\|PDB:2OBV

Chain	Residue	Details
A	HIS29
D	HIS29
D	ASP179
D	SER247
A	ASP179
A	SER247
B	HIS29
B	ASP179
B	SER247
C	HIS29
C	ASP179
C	SER247

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P0A817

Chain	Residue	Details
A	GLU57
C	ASP258
C	ALA281
C	LYS285
D	GLU57
D	ASP258
D	ALA281
D	LYS285
A	ASP258
A	ALA281
A	LYS285
B	GLU57
B	ASP258
B	ALA281
B	LYS285
C	GLU57

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: in other chain => ECO:0000250\|UniProtKB:P0A817

Chain	Residue	Details
A	GLU70
C	GLN113
C	ARG264
C	LYS289
D	GLU70
D	GLN113
D	ARG264
D	LYS289
A	GLN113
A	ARG264
A	LYS289
B	GLU70
B	GLN113
B	ARG264
B	LYS289
C	GLU70

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000250\|UniProtKB:P13444

Chain	Residue	Details
A	CYS120
B	CYS120
C	CYS120
D	CYS120

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)