Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FMO

Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 900

Chain	Residue
A	ARG230
A	PRO232
A	ALA233
A	TRP234

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 901

Chain	Residue
A	SER44
A	ARG279
A	ALA280
A	GLU281
A	HOH533

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 902

Chain	Residue
B	SER44
B	ARG279
B	ALA280
B	GLU281
B	HOH452
B	HOH564

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 903

Chain	Residue
B	SER215
B	ASN216
B	ARG249
B	HOH565

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 904

Chain	Residue
C	ARG279
C	ALA280
C	GLU281
C	HOH511
C	HOH593

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD A 395

Chain	Residue
A	THR59
A	TYR60
A	ALA62
A	HIS88
A	THR90
A	LEU117
A	ARG118
A	GLY119
A	ASP120
A	TYR131
A	ALA132
A	ALA150
A	TYR152
A	HIS156
A	GLU158
A	ALA159
A	ASP165
A	ARG171
A	LYS172
A	ILE181
A	TYR275
A	HOH522
A	HOH607

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD B 396

Chain	Residue
B	THR59
B	TYR60
B	ALA62
B	HIS88
B	LEU117
B	ARG118
B	GLY119
B	ASP120
B	TYR131
B	ALA132
B	ALA150
B	TYR152
B	HIS156
B	GLU158
B	ALA159
B	ASP165
B	ASN168
B	ARG171
B	LYS172
B	ILE181
B	TYR275
B	HOH429
B	HOH431
B	HOH435
B	HOH527
B	HOH546

site_id	AC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD C 397

Chain	Residue
C	THR59
C	TYR60
C	HIS88
C	LEU117
C	ARG118
C	GLY119
C	ASP120
C	TYR131
C	ALA132
C	SER133
C	ALA150
C	TYR152
C	HIS156
C	ALA159
C	ASP165
C	ASN168
C	LYS172
C	ILE181
C	GLN183
C	TYR275
C	HOH413
C	HOH465
C	HOH473
C	HOH474
C	HOH650

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD A 895

Chain	Residue
A	TYR275
A	PHE223

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD B 896

Chain	Residue
B	PHE223
B	TYR275
B	HOH630

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD C 897

Chain	Residue
C	PHE223
C	TYR275
C	LEU277
C	HOH421
C	HOH645

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	6
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	GLU28
A	ASP120

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

Chain	Residue	Details
B	GLU28
B	ASP120

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

Chain	Residue	Details
C	GLU28
C	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	PHE223	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
B	SER26	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	GLU28	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
B	ASP120	electrostatic stabiliser, hydrogen bond acceptor
B	PHE223	steric locator
B	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
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	PHE223	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)