Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UGH

Crystal structure of Mat2a bound to the allosteric inhibitor PF-02929366

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
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	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	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	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	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	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	14
Details	binding site for residue 8AJ A 401

Chain	Residue
A	LEU315
C	PHE18
C	PHE20
C	GLN190
C	GLY273
C	TRP274
A	GLN317
A	SER331
A	ILE332
A	PHE333
A	GLU342
C	GLU15
C	GLY16
C	THR17

site_id	AC2
Number of Residues	14
Details	binding site for residue 8AJ B 401

Chain	Residue
B	GLN317
B	SER331
B	ILE332
B	PHE333
B	GLU342
B	HOH547
D	GLU15
D	GLY16
D	THR17
D	PHE18
D	PHE20
D	GLN190
D	GLY273
D	TRP274

site_id	AC3
Number of Residues	11
Details	binding site for residue 8AJ B 402

Chain	Residue
B	PHE18
B	PHE20
B	GLN190
B	GLY273
B	TRP274
B	HOH535
D	LEU315
D	SER331
D	ILE332
D	PHE333
D	GLU342

site_id	AC4
Number of Residues	13
Details	binding site for residue 8AJ C 401

Chain	Residue
A	GLU15
A	PHE18
A	PHE20
A	GLN190
A	GLY273
A	TRP274
C	LEU315
C	GLN317
C	SER331
C	ILE332
C	PHE333
C	GLU342
C	HOH534

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	8
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
B	HIS29
B	ARG264
C	HIS29
C	ARG264
D	HIS29
D	ARG264

site_id	SWS_FT_FI2
Number of Residues	4
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
B	ASP31
C	ASP31
D	ASP31

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P0A817

Chain	Residue	Details
A	GLU57
B	GLU57
C	GLU57
D	GLU57

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

Chain	Residue	Details
A	GLU70
B	GLU70
C	GLU70
D	GLU70

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: in other chain => ECO:0000305\|PubMed:25075345

Chain	Residue	Details
A	GLN113
B	GLN113
C	GLN113
D	GLN113

site_id	SWS_FT_FI6
Number of Residues	4
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
B	ASP179
C	ASP179
D	ASP179

site_id	SWS_FT_FI7
Number of Residues	4
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
B	SER247
C	SER247
D	SER247

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

Chain	Residue	Details
A	ASP258
B	ASP258
C	ASP258
D	ASP258

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

Chain	Residue	Details
A	ALA281
B	ALA281
C	ALA281
D	ALA281

site_id	SWS_FT_FI10
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:25075345, ECO:0000305\|PubMed:26858410, ECO:0007744\|PDB:4NDN

Chain	Residue	Details
A	LYS285
A	ASP291
B	LYS285
B	ASP291
C	LYS285
C	ASP291
D	LYS285
D	ASP291

site_id	SWS_FT_FI11
Number of Residues	4
Details	BINDING: in other chain => ECO:0000250\|UniProtKB:P0A817

Chain	Residue	Details
A	LYS289
B	LYS289
C	LYS289
D	LYS289

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS81
B	LYS81
C	LYS81
D	LYS81

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
A	SER114
B	SER114
C	SER114
D	SER114

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER384
B	SER384
C	SER384
D	SER384

site_id	SWS_FT_FI15
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS228
D	LYS228
D	LYS234
A	LYS234
B	LYS228
B	LYS234
C	LYS228
C	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

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)