Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FST

Crystal Structure of Escherichia coli Methylenetetrahydrofolate Reductase Mutant Phe223Leu at pH 7.4

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	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	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	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	ALA132
A	ALA150
A	TYR152
A	HIS156
A	GLU158
A	ALA159
A	ASP165
A	ASN168
A	ARG171
A	LYS172
A	TYR60
A	ILE181
A	GLN183
A	TYR275
A	HOH322
A	HOH336
A	HOH363
A	HOH367
A	HOH402
A	HOH438
A	ALA62
A	HIS88
A	LEU117
A	ARG118
A	GLY119
A	ASP120
A	TYR131

site_id	AC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD C 396

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	HOH340
C	HOH343
C	HOH375
C	HOH393
C	HOH450
C	HOH488
C	HOH491
C	HOH517
C	MRY5321

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD E 397

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	ALA159
E	ASP165
E	ASN168
E	ARG171
E	LYS172
E	ILE181
E	GLN183
E	TYR275
E	HOH315
E	HOH447

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MRY C 5321

Chain	Residue
C	GLU28
C	GLN183
C	PHE184
C	TYR275
C	LEU277
C	HOH360
C	HOH394
C	FAD396
C	HOH459

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 305

Chain	Residue
E	ARG230
E	PRO232
E	ALA233
E	TRP234
E	HOH465

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 306

Chain	Residue
A	HOH426
E	HOH520
A	ARG279
A	ALA280
A	GLU281
A	HOH318

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 307

Chain	Residue
E	SER44
E	ARG279
E	ALA280
E	GLU281
E	HOH329
E	HOH521

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor/acceptor => ECO:0000305\|PubMed:11371182, ECO:0000305\|PubMed:16114881

Chain	Residue	Details
A	GLU28
C	GLU28
E	GLU28

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269\|PubMed:16114881, ECO:0007744\|PDB:1ZPT

Chain	Residue	Details
A	THR59
A	ALA159
A	GLN183
C	THR59
C	ALA159
C	GLN183
E	THR59
E	ALA159
E	GLN183

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:16114881, ECO:0000269\|PubMed:19610625, ECO:0007744\|PDB:1ZPT, ECO:0007744\|PDB:3FST, ECO:0007744\|PDB:3FSU

Chain	Residue	Details
A	TYR60
A	LYS172
C	TYR60
C	HIS88
C	ARG118
C	GLY119
C	ALA132
C	TYR152
C	HIS156
C	ASN168
C	ARG171
A	HIS88
C	LYS172
E	TYR60
E	HIS88
E	ARG118
E	GLY119
E	ALA132
E	TYR152
E	HIS156
E	ASN168
E	ARG171
A	ARG118
E	LYS172
A	GLY119
A	ALA132
A	TYR152
A	HIS156
A	ASN168
A	ARG171

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:19610625, ECO:0007744\|PDB:3FST, ECO:0007744\|PDB:3FSU

Chain	Residue	Details
A	ALA62
A	ASP120
C	ALA62
C	ASP120
E	ALA62
E	ASP120

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16114881, ECO:0000269\|PubMed:19610625, ECO:0007744\|PDB:1ZPT, ECO:0007744\|PDB:3FST

Chain	Residue	Details
A	ASP165
C	ASP165
E	ASP165

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16114881, ECO:0007744\|PDB:1ZP4

Chain	Residue	Details
A	GLN219
C	GLN219
E	GLN219

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:16114881, ECO:0000269\|PubMed:19610625, ECO:0007744\|PDB:3FSU

Chain	Residue	Details
A	ARG279
C	ARG279
E	ARG279

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU28
A	ASP120

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

Chain	Residue	Details
C	GLU28
C	ASP120

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

Chain	Residue	Details
E	GLU28
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	GLU28	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
C	SER26	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
C	GLU28	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

site_id	MCSA3
Number of Residues	5
Details	M-CSA 120

Chain	Residue	Details
E	SER26	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
E	GLU28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
E	ASP120	electrostatic stabiliser, hydrogen bond acceptor
E	LEU223	steric locator
E	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)