Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FBP

Human Methionine Adenosyltransferase II mutant (S114A) in P22121 crystal form

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	0031503	biological_process	protein-containing complex localization
A	0031669	biological_process	cellular response to nutrient levels
A	0034198	biological_process	cellular response to amino acid starvation
A	0034214	biological_process	protein hexamerization
A	0036094	molecular_function	small molecule binding
A	0038202	biological_process	TORC1 signaling
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	0061462	biological_process	protein localization to lysosome
A	1904262	biological_process	negative regulation of TORC1 signaling
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	0031503	biological_process	protein-containing complex localization
B	0031669	biological_process	cellular response to nutrient levels
B	0034198	biological_process	cellular response to amino acid starvation
B	0034214	biological_process	protein hexamerization
B	0036094	molecular_function	small molecule binding
B	0038202	biological_process	TORC1 signaling
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	0061462	biological_process	protein localization to lysosome
B	1904262	biological_process	negative regulation of TORC1 signaling
B	1904263	biological_process	positive regulation of TORC1 signaling
B	1990830	biological_process	cellular response to leukemia inhibitory factor

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue PG4 A 401

Chain	Residue
A	PHE18
B	PG4403
A	GLN190
A	TRP274
A	GLY275
A	ARG313
A	HOH542
A	HOH574
B	GLN317
B	PHE333

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

Chain	Residue
A	GLU148
A	VAL155
A	LYS159
A	PRO232
A	HOH635

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO A 403

Chain	Residue
A	LYS228
A	ALA229

site_id	AC4
Number of Residues	3
Details	binding site for residue K A 404

Chain	Residue
A	ALA233
A	LEU236
A	HOH576

site_id	AC5
Number of Residues	4
Details	binding site for residue MG A 405

Chain	Residue
A	ASP291
A	HOH502
A	HOH537
B	PPK401

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO A 406

Chain	Residue
A	GLN48
A	PRO50
A	HOH515
B	GLN48
B	PRO50

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO A 407

Chain	Residue
A	GLY16
A	GLU238

site_id	AC8
Number of Residues	21
Details	binding site for residue PPK B 401

Chain	Residue
A	ASP134
A	GLY280
A	ALA281
A	LYS285
A	ASP291
A	MG405
A	HOH537
A	HOH609
B	HIS29
B	ASP31
B	LYS181
B	ARG264
B	LYS265
B	MG402
B	ADN404
B	K405
B	HOH508
B	HOH512
B	HOH527
B	HOH534
B	HOH545

site_id	AC9
Number of Residues	5
Details	binding site for residue MG B 402

Chain	Residue
B	ASP31
B	LYS265
B	PPK401
B	HOH527
B	HOH545

site_id	AD1
Number of Residues	9
Details	binding site for residue PG4 B 403

Chain	Residue
A	PHE333
A	TYR335
A	PG4401
B	GLN190
B	VAL195
B	ARG313
B	TYR335
B	HOH550
B	HOH659

site_id	AD2
Number of Residues	15
Details	binding site for residue ADN B 404

Chain	Residue
A	ASP116
A	ILE117
A	ASP134
A	ILE322
A	HOH677
B	HIS29
B	PRO30
B	ASP179
B	LYS181
B	SER247
B	ARG249
B	PHE250
B	ASP258
B	PPK401
B	HOH520

site_id	AD3
Number of Residues	5
Details	binding site for residue K B 405

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

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	24
Details	Region: {"description":"Flexible loop","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
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_FI3
Number of Residues	2
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_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
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_FI6
Number of Residues	2
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
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_FI8
Number of Residues	6
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_FI9
Number of Residues	2
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_FI10
Number of Residues	2
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_FI11
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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	6
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

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