Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7BHX

Crystal structure of MAT2a bound to allosteric inhibitor (compound 31)

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	8
Details	binding site for residue DMS A 401

Chain	Residue
A	ASP124
A	ARG125
A	ASN126
A	LYS228
A	ALA229
A	VAL230
A	VAL231
A	HOH533

site_id	AC2
Number of Residues	15
Details	binding site for residue TO5 A 402

Chain	Residue
A	PHE20
A	GLY273
A	TRP274
A	GLY275
A	GLY275
A	ARG313
A	LEU315
A	SER331
A	ILE332
A	PHE333
A	TYR335
A	HOH507
A	HOH507
A	HOH664
A	PHE18

site_id	AC3
Number of Residues	24
Details	binding site for residue SAM A 403

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	ILE322
A	CL404
A	HOH550
A	HOH626
A	HOH635
A	HOH640
A	HOH726
A	HOH731

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

Chain	Residue
A	HIS29
A	ASP134
A	LYS181
A	LYS265
A	SAM403

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)