Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FSU

Crystal Structure of Escherichia coli Methylenetetrahydrofolate Reductase Double Mutant Phe223LeuGlu28Gln complexed with methyltetrahydrofolate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004489	molecular_function	methylenetetrahydrofolate reductase [NAD(P)H] activity
A	0005829	cellular_component	cytosol
A	0006555	biological_process	methionine metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0009086	biological_process	methionine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0032991	cellular_component	protein-containing complex
A	0035999	biological_process	tetrahydrofolate interconversion
A	0051087	molecular_function	protein-folding chaperone binding
A	0071949	molecular_function	FAD binding
A	0106312	molecular_function	methylenetetrahydrofolate reductase (NADH) activity
C	0004489	molecular_function	methylenetetrahydrofolate reductase [NAD(P)H] activity
C	0005829	cellular_component	cytosol
C	0006555	biological_process	methionine metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0009086	biological_process	methionine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0032991	cellular_component	protein-containing complex
C	0035999	biological_process	tetrahydrofolate interconversion
C	0051087	molecular_function	protein-folding chaperone binding
C	0071949	molecular_function	FAD binding
C	0106312	molecular_function	methylenetetrahydrofolate reductase (NADH) activity
E	0004489	molecular_function	methylenetetrahydrofolate reductase [NAD(P)H] activity
E	0005829	cellular_component	cytosol
E	0006555	biological_process	methionine metabolic process
E	0008652	biological_process	amino acid biosynthetic process
E	0009086	biological_process	methionine biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0032991	cellular_component	protein-containing complex
E	0035999	biological_process	tetrahydrofolate interconversion
E	0051087	molecular_function	protein-folding chaperone binding
E	0071949	molecular_function	FAD binding
E	0106312	molecular_function	methylenetetrahydrofolate reductase (NADH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD A 395

Chain	Residue
A	THR59
A	TYR131
A	ALA132
A	ALA150
A	TYR152
A	HIS156
A	GLU158
A	ALA159
A	ASP165
A	ASN168
A	ARG171
A	TYR60
A	LYS172
A	ILE181
A	GLN183
A	TYR275
A	HOH322
A	HOH338
A	HOH364
A	HOH368
A	C2F995
A	ALA62
A	HIS88
A	THR90
A	LEU117
A	ARG118
A	GLY119
A	ASP120

site_id	AC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD C 395

Chain	Residue
C	THR59
C	TYR60
C	HIS88
C	LEU117
C	ARG118
C	GLY119
C	ASP120
C	TYR131
C	ALA132
C	ALA150
C	TYR152
C	HIS156
C	GLU158
C	ALA159
C	ASP165
C	ASN168
C	ARG171
C	LYS172
C	ILE181
C	GLN183
C	TYR275
C	HOH341
C	HOH344
C	HOH382
C	HOH398
C	HOH426
C	HOH454
C	HOH456
C	HOH477
C	MRY5320

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD E 395

Chain	Residue
E	THR59
E	TYR60
E	HIS88
E	THR90
E	LEU117
E	ARG118
E	GLY119
E	ASP120
E	TYR131
E	ALA132
E	ALA150
E	TYR152
E	HIS156
E	GLU158
E	ALA159
E	ASP165
E	ASN168
E	ARG171
E	LYS172
E	ILE181
E	GLN183
E	TYR275
E	HOH315
E	HOH350
E	C2F995

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE C2F A 995

Chain	Residue
A	GLN28
A	ASP120
A	GLN183
A	SER215
A	GLN219
A	LEU223
A	THR227
A	TYR275
A	LEU277
A	ARG279
A	HOH364
A	HOH366
A	HOH389
A	FAD395
A	HOH406
A	HOH452

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE C2F E 995

Chain	Residue
E	GLN28
E	ASP120
E	GLN183
E	SER215
E	GLN219
E	LEU223
E	THR227
E	TYR275
E	LEU277
E	ARG279
E	HOH336
E	HOH348
E	HOH350
E	HOH394
E	FAD395

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MRY C5320

Chain	Residue
C	GLN28
C	GLN183
C	PHE184
C	LEU277
C	HOH356
C	HOH359
C	HOH360
C	FAD395
C	HOH399

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 305

Chain	Residue
E	ARG230
E	PRO232
E	ALA233
E	TRP234

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"11371182","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16114881","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16114881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16114881","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19610625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FSU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19610625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FST","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FSU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16114881","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19610625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZPT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FST","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16114881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZP4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16114881","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19610625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FSU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1b5t

Chain	Residue	Details
A	GLN28
A	ASP120

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1b5t

Chain	Residue	Details
C	GLN28
C	ASP120

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1b5t

Chain	Residue	Details
E	GLN28
E	ASP120

site_id	MCSA1
Number of Residues	5
Details	M-CSA 120

Chain	Residue	Details
A	SER26	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	GLN28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ASP120	electrostatic stabiliser, hydrogen bond acceptor
A	LEU223	steric locator
A	HIS273	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

site_id	MCSA2
Number of Residues	5
Details	M-CSA 120

Chain

Residue

Details

site_id	MCSA3
Number of Residues	5
Details	M-CSA 120

Chain	Residue	Details
C	SER26	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	GLN28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	ASP120	electrostatic stabiliser, hydrogen bond acceptor
C	LEU223	steric locator
C	HIS273	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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