Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6G6R

Human Methionine Adenosyltransferase II with SAMe and PPNP

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	0016740	molecular_function	transferase activity
A	0034214	biological_process	protein hexamerization
A	0036094	molecular_function	small molecule binding
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048269	cellular_component	methionine adenosyltransferase complex
A	0051291	biological_process	protein heterooligomerization
A	0061431	biological_process	cellular response to methionine
A	1904263	biological_process	positive regulation of TORC1 signaling
A	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue PPK A 401

Chain	Residue
A	HIS29
A	ASP291
A	MG402
A	MG403
A	K404
A	SAM406
A	HOH506
A	HOH509
A	HOH533
A	HOH536
A	HOH538
A	ASP31
A	HOH541
A	HOH552
A	HOH573
A	HOH624
A	ASP134
A	LYS181
A	ARG264
A	LYS265
A	GLY280
A	ALA281
A	LYS285

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 402

Chain	Residue
A	ASP31
A	LYS265
A	PPK401
A	HOH538
A	HOH552

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 403

Chain	Residue
A	PPK401
A	HOH533
A	HOH536
A	HOH573
A	HOH624

site_id	AC4
Number of Residues	5
Details	binding site for residue K A 404

Chain	Residue
A	GLU57
A	ASP258
A	ALA259
A	PPK401
A	HOH553

site_id	AC5
Number of Residues	6
Details	binding site for residue K A 405

Chain	Residue
A	MET138
A	PHE139
A	HIS277
A	GLY278
A	HOH665
A	HOH751

site_id	AC6
Number of Residues	23
Details	binding site for residue SAM A 406

Chain	Residue
A	HIS29
A	PRO30
A	ALA55
A	GLU70
A	GLN113
A	ASP116
A	ILE117
A	GLY133
A	ASP134
A	ASP179
A	LYS181
A	SER247
A	ARG249
A	PHE250
A	ASP258
A	LYS289
A	PPK401
A	HOH509
A	HOH565
A	HOH579
A	HOH618
A	HOH622
A	HOH716

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

Chain	Residue
A	HOH587
A	HOH621
A	HOH641
A	HOH730

site_id	AC8
Number of Residues	7
Details	binding site for residue PG4 A 408

Chain	Residue
A	GLN36
A	HIS89
A	GLN372
A	ARG373
A	TYR377
A	HOH613
A	HOH737

site_id	AC9
Number of Residues	5
Details	binding site for residue PG4 A 409

Chain	Residue
A	PHE18
A	GLN190
A	ARG313
A	PHE333
A	TYR335

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	2
Details	BINDING: in other chain => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4NDN, ECO:0007744\|PDB:5A19

Chain	Residue	Details
A	HIS29
A	ARG264

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4KTT, ECO:0007744\|PDB:4NDN, ECO:0007744\|PDB:5A19, ECO:0007744\|PDB:5A1G, ECO:0007744\|PDB:5A1I

Chain	Residue	Details
A	ASP31

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P0A817

Chain	Residue	Details
A	GLU57

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: in other chain => ECO:0000305\|PubMed:25075345, ECO:0007744\|PDB:4NDN

Chain	Residue	Details
A	GLU70

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: in other chain => ECO:0000305\|PubMed:25075345

Chain	Residue	Details
A	GLN113

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: in other chain => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4KTT, ECO:0007744\|PDB:4NDN, ECO:0007744\|PDB:5A19, ECO:0007744\|PDB:5A1G, ECO:0007744\|PDB:5A1I

Chain	Residue	Details
A	ASP179

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: in other chain => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4KTT, ECO:0007744\|PDB:4NDN, ECO:0007744\|PDB:5A1G, ECO:0007744\|PDB:5A1I

Chain	Residue	Details
A	SER247

site_id	SWS_FT_FI8
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4NDN, ECO:0007744\|PDB:5A1I

Chain	Residue	Details
A	ASP258

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305\|PubMed:25075345, ECO:0007744\|PDB:4NDN

Chain	Residue	Details
A	ALA281

site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4NDN

Chain	Residue	Details
A	LYS285
A	ASP291

site_id	SWS_FT_FI11
Number of Residues	1
Details	BINDING: in other chain => ECO:0000250\|UniProtKB:P0A817

Chain	Residue	Details
A	LYS289

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS81

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER114

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER384

site_id	SWS_FT_FI15
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS228
A	LYS234

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	14
Details	M-CSA 9

Chain	Residue	Details
A	HIS29	proton acceptor, proton donor
A	ARG264	electrostatic stabiliser
A	LYS265	electrostatic stabiliser
A	LYS285	electrostatic stabiliser
A	LYS289	electrostatic stabiliser
A	ASP291	electrostatic stabiliser
A	ASP31	electrostatic stabiliser, metal ligand
A	LYS32	electrostatic stabiliser
A	GLU57	metal ligand
A	GLU70	electrostatic stabiliser, steric role
A	LYS181	electrostatic stabiliser
A	PHE250	steric role
A	ASP258	electrostatic stabiliser, metal ligand, steric role
A	ALA259	metal ligand

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