Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FWB

Crystal structure of Mat2A at 1.79 Angstron resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0051259	biological_process	protein complex oligomerization
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
B	0000166	molecular_function	nucleotide binding
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	0016740	molecular_function	transferase activity
B	0034214	biological_process	protein hexamerization
B	0036094	molecular_function	small molecule binding
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048269	cellular_component	methionine adenosyltransferase complex
B	0051259	biological_process	protein complex oligomerization
B	0051291	biological_process	protein heterooligomerization
B	0061431	biological_process	cellular response to methionine
B	1904263	biological_process	positive regulation of TORC1 signaling
B	1990830	biological_process	cellular response to leukemia inhibitory factor
C	0000166	molecular_function	nucleotide binding
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	0016740	molecular_function	transferase activity
C	0034214	biological_process	protein hexamerization
C	0036094	molecular_function	small molecule binding
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048269	cellular_component	methionine adenosyltransferase complex
C	0051259	biological_process	protein complex oligomerization
C	0051291	biological_process	protein heterooligomerization
C	0061431	biological_process	cellular response to methionine
C	1904263	biological_process	positive regulation of TORC1 signaling
C	1990830	biological_process	cellular response to leukemia inhibitory factor
D	0000166	molecular_function	nucleotide binding
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	0016740	molecular_function	transferase activity
D	0034214	biological_process	protein hexamerization
D	0036094	molecular_function	small molecule binding
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0048269	cellular_component	methionine adenosyltransferase complex
D	0051259	biological_process	protein complex oligomerization
D	0051291	biological_process	protein heterooligomerization
D	0061431	biological_process	cellular response to methionine
D	1904263	biological_process	positive regulation of TORC1 signaling
D	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue SO4 B 401

Chain	Residue
B	LYS228
B	ALA229
B	VAL230
B	VAL231
B	PRO232

site_id	AC2
Number of Residues	3
Details	binding site for residue SO4 B 402

Chain	Residue
B	ILE348
B	LEU393
B	LYS394

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 B 403

Chain	Residue
B	GLY323
B	VAL324
B	SER325
B	ASP129

site_id	AC4
Number of Residues	6
Details	binding site for residue SO4 B 404

Chain	Residue
B	LYS350
B	LYS351
B	ASN352
B	PHE353
B	ASP354
B	HOH505

site_id	AC5
Number of Residues	3
Details	binding site for residue SO4 B 405

Chain	Residue
B	GLU148
B	LEU152
B	LYS159

site_id	AC6
Number of Residues	6
Details	binding site for residue SO4 B 406

Chain	Residue
B	MET138
B	PHE139
B	HIS277
B	GLY278
B	ALA295
B	HOH586

site_id	AC7
Number of Residues	6
Details	binding site for residue SO4 B 407

Chain	Residue
B	SER95
B	SER96
B	GLY98
B	GLN256
B	HOH522
D	LYS102

site_id	AC8
Number of Residues	6
Details	binding site for residue PG4 B 408

Chain	Residue
B	GLN80
B	ARG84
B	GLU85
C	GLU111
D	GLN256
D	PG4406

site_id	AC9
Number of Residues	6
Details	binding site for residue PG4 B 409

Chain	Residue
B	GLN372
B	ARG373
B	ALA376
B	TYR377
B	ARG382
B	HOH607

site_id	AD1
Number of Residues	6
Details	binding site for residue NA B 410

Chain	Residue
B	ASP43
B	PRO369
B	ILE370
B	TYR371
B	GLN372
B	ARG373

site_id	AD2
Number of Residues	8
Details	binding site for residue GOL A 401

Chain	Residue
A	GLY26
A	GLU27
A	ASN161
A	ARG168
A	ARG177
A	PRO178
A	SER180
A	TYR377

site_id	AD3
Number of Residues	9
Details	binding site for residue SO4 A 402

Chain	Residue
A	ASP31
A	ARG264
A	LYS265
A	HOH509
A	HOH513
A	HOH519
B	GLY280
B	ALA281
B	LYS285

site_id	AD4
Number of Residues	5
Details	binding site for residue SO4 A 403

Chain	Residue
A	THR146
A	GLU148
A	VAL155
A	LYS159
A	PRO232

site_id	AD5
Number of Residues	6
Details	binding site for residue SO4 A 404

Chain	Residue
A	LYS228
A	ALA229
A	VAL230
A	VAL231
A	PRO232
A	HOH603

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 A 405

Chain	Residue
A	LYS350
A	LYS351
A	ASN352
A	PHE353
A	ASP354

site_id	AD7
Number of Residues	4
Details	binding site for residue SO4 A 406

Chain	Residue
A	ASP239
A	THR240
A	ILE241
A	HOH580

site_id	AD8
Number of Residues	3
Details	binding site for residue SO4 A 407

Chain	Residue
A	SER247
A	ARG249
A	PHE250

site_id	AD9
Number of Residues	7
Details	binding site for residue SO4 A 408

Chain	Residue
A	CYS214
A	LEU215
A	ARG249
A	HOH514
A	HOH610
A	HOH617
B	LEU215

site_id	AE1
Number of Residues	6
Details	binding site for residue SO4 A 409

Chain	Residue
A	ILE332
A	GLU342
A	HOH504
B	THR17
B	PHE18
A	SER331

site_id	AE2
Number of Residues	9
Details	binding site for residue PG4 A 410

Chain	Residue
A	PHE20
A	GLN190
A	TRP274
A	GLY275
A	ARG313
A	TYR335
A	HOH546
A	HOH573
B	GLN317

site_id	AE3
Number of Residues	5
Details	binding site for residue PG4 A 411

Chain	Residue
A	PHE333
A	HOH546
B	GLN190
B	TRP274
B	ARG313

site_id	AE4
Number of Residues	7
Details	binding site for residue PG4 C 401

Chain	Residue
C	PHE18
C	GLN190
C	TRP274
C	ARG313
D	PHE333
D	TYR335
D	PG4407

site_id	AE5
Number of Residues	9
Details	binding site for residue GOL D 401

Chain	Residue
D	GLY26
D	GLU27
D	ASN161
D	ALA165
D	ARG168
D	ARG177
D	PRO178
D	SER180
D	TYR377

site_id	AE6
Number of Residues	5
Details	binding site for residue SO4 D 402

Chain	Residue
D	HIS334
D	SER338
D	GLN339
D	LYS340
D	SER341

site_id	AE7
Number of Residues	6
Details	binding site for residue SO4 D 403

Chain	Residue
D	LYS228
D	ALA229
D	VAL230
D	VAL231
D	PRO232
D	HOH516

site_id	AE8
Number of Residues	8
Details	binding site for residue SO4 D 404

Chain	Residue
C	GLY280
C	ALA281
C	LYS285
D	ASP31
D	ARG264
D	LYS265
D	HOH539
D	HOH546

site_id	AE9
Number of Residues	7
Details	binding site for residue SO4 D 405

Chain	Residue
D	MET138
D	PHE139
D	ALA276
D	HIS277
D	GLY278
D	ALA295
D	HOH540

site_id	AF1
Number of Residues	4
Details	binding site for residue PG4 D 406

Chain	Residue
B	LYS102
B	PG4408
D	ILE252
D	GLN256

site_id	AF2
Number of Residues	6
Details	binding site for residue PG4 D 407

Chain	Residue
C	PG4401
D	PHE18
D	GLN190
D	GLY275
D	ARG313
D	HOH510

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
B	GLY131-TYR141

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

Chain	Residue	Details
B	GLY278-ASP286

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	12
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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

site_id	MCSA2
Number of Residues	14
Details	M-CSA 9

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

site_id	MCSA3
Number of Residues	14
Details	M-CSA 9

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

site_id	MCSA4
Number of Residues	14
Details	M-CSA 9

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

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