Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1P7L

S-Adenosylmethionine synthetase complexed with AMPPNP and Met.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 386

Chain	Residue
A	ASP238
A	CYS239
A	ANP384
B	GLU42

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 387

Chain	Residue
A	LYS245
A	ANP384

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 388

Chain	Residue
A	ASP16
A	ANP384

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 486

Chain	Residue
B	ASP238
B	CYS239
B	ANP484
A	GLU42

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 487

Chain	Residue
B	LYS245
B	ANP484

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 488

Chain	Residue
B	ASP16
B	ANP484

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C 686

Chain	Residue
C	ASP238
C	CYS239
C	PPK684
D	GLU42

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 687

Chain	Residue
C	PPK684
D	ASP118
D	ASP271

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 688

Chain	Residue
C	ASP16
C	PPK684

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 886

Chain	Residue
C	GLU42
D	ASP238
D	CYS239
D	PPK884

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 887

Chain	Residue
C	ASP271
D	PPK884

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 888

Chain	Residue
D	ASP16
D	PPK884

site_id	BC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE SAM C 685

Chain	Residue
C	HIS14
C	PRO15
C	ASP163
C	LYS165
C	THR227
C	ARG229
C	PHE230
C	ASP238
C	PPK684
C	HOH700
C	HOH702
C	HOH711
C	HOH716
D	ALA40
D	GLU55
D	GLN98
D	ASP101
D	ILE102
D	GLY117
D	ASP118
D	LYS269
D	ILE302

site_id	BC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE SAM C 885

Chain	Residue
C	ALA40
C	GLU55
C	GLN98
C	ASP101
C	ILE102
C	GLY117
C	ASP118
C	LYS269
C	ILE302
C	HOH900
C	HOH902
D	HIS14
D	PRO15
D	ASP163
D	LYS165
D	THR227
D	ARG229
D	PHE230
D	ASP238
D	PPK884
D	HOH916

site_id	BC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ANP A 384

Chain	Residue
B	MET385
A	HIS14
A	PRO15
A	ASP16
A	ASP163
A	LYS165
A	SER186
A	ARG229
A	PHE230
A	ASP238
A	ARG244
A	LYS245
A	K386
A	MG387
A	MG388
A	HOH411
A	HOH413
B	ILE102
B	ASP118
B	GLY259
B	GLY260
B	ALA261
B	LYS265
B	ASP271

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MET B 385

Chain	Residue
A	ASP238
A	ANP384
A	HOH401
B	ALA40
B	GLU55
B	GLN98
B	ILE102
B	GLY117
B	ASP118
B	LYS269
B	ILE302
B	HOH400

site_id	BC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP B 484

Chain	Residue
A	ASP101
A	ILE102
A	ASP118
A	GLY259
A	GLY260
A	ALA261
A	LYS265
A	ASP271
A	MET485
A	HOH530
B	HIS14
B	PRO15
B	ASP16
B	ASP163
B	LYS165
B	SER186
B	ARG229
B	PHE230
B	ASP238
B	ARG244
B	LYS245
B	K486
B	MG487
B	MG488
B	HOH513

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MET A 485

Chain	Residue
A	ALA40
A	GLU55
A	GLN98
A	ILE102
A	GLY117
A	ASP118
A	LYS269
A	ILE302
A	HOH500
A	HOH501
B	ASP238
B	ANP484

site_id	CC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PPK C 684

Chain	Residue
C	HIS14
C	ASP16
C	LYS165
C	ARG244
C	LYS245
C	SAM685
C	K686
C	MG688
D	ASP118
D	GLY259
D	GLY260
D	ALA261
D	LYS265
D	ASP271
D	MG687

site_id	CC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PPK D 884

Chain	Residue
C	ASP118
C	GLY259
C	GLY260
C	ALA261
C	LYS265
C	ASP271
C	SAM885
C	MG887
C	HOH930
D	HIS14
D	ASP16
D	LYS165
D	ARG244
D	LYS245
D	K886
D	MG888

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

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

Chain	Residue	Details
A	GLY258-ASP266

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
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	PRO15
B	SER99
B	ALA164
B	PHE230
B	LYS245
B	VAL270
C	PRO15
C	ILE56
C	SER99
C	ALA164
C	PHE230
A	ILE56
C	LYS245
C	VAL270
D	PRO15
D	ILE56
D	SER99
D	ALA164
D	PHE230
D	LYS245
D	VAL270
A	SER99
A	ALA164
A	PHE230
A	LYS245
A	VAL270
B	PRO15
B	ILE56

site_id	SWS_FT_FI2
Number of Residues	12
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	LYS17
D	LYS17
D	PHE262
D	ASP266
A	PHE262
A	ASP266
B	LYS17
B	PHE262
B	ASP266
C	LYS17
C	PHE262
C	ASP266

site_id	SWS_FT_FI3
Number of Residues	4
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	THR43
B	THR43
C	THR43
D	THR43

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00086, ECO:0000269\|PubMed:14967023, ECO:0007744\|PDB:1P7L

Chain	Residue	Details
A	CYS239
B	CYS239
C	CYS239
D	CYS239

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	HIS3
B	HIS3
C	HIS3
D	HIS3

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS245
A	HIS14
A	LYS165
A	ARG244
B	LYS269
B	LYS265
B	ASP271

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

Chain	Residue	Details
A	LYS269
A	LYS265
A	ASP271
B	LYS245
B	HIS14
B	LYS165
B	ARG244

site_id	CSA3
Number of Residues	7
Details	Annotated By Reference To The Literature 1fug

Chain	Residue	Details
C	LYS245
C	HIS14
C	LYS165
C	ARG244
D	LYS269
D	LYS265
D	ASP271

site_id	CSA4
Number of Residues	7
Details	Annotated By Reference To The Literature 1fug

Chain	Residue	Details
C	LYS269
C	LYS265
C	ASP271
D	LYS245
D	HIS14
D	LYS165
D	ARG244

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)