Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UME

Crystal Structure of 5,10-Methylenetetrahydrofolate Reductase MetF from Haemophilus influenzae

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	0035999	biological_process	tetrahydrofolate interconversion
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	0035999	biological_process	tetrahydrofolate interconversion
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	0035999	biological_process	tetrahydrofolate interconversion
C	0071949	molecular_function	FAD binding
C	0106312	molecular_function	methylenetetrahydrofolate reductase (NADH) activity
D	0004489	molecular_function	methylenetetrahydrofolate reductase [NAD(P)H] activity
D	0005829	cellular_component	cytosol
D	0006555	biological_process	methionine metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0009086	biological_process	methionine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0035999	biological_process	tetrahydrofolate interconversion
D	0071949	molecular_function	FAD binding
D	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	0035999	biological_process	tetrahydrofolate interconversion
E	0071949	molecular_function	FAD binding
E	0106312	molecular_function	methylenetetrahydrofolate reductase (NADH) activity
F	0004489	molecular_function	methylenetetrahydrofolate reductase [NAD(P)H] activity
F	0005829	cellular_component	cytosol
F	0006555	biological_process	methionine metabolic process
F	0008652	biological_process	amino acid biosynthetic process
F	0009086	biological_process	methionine biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0035999	biological_process	tetrahydrofolate interconversion
F	0071949	molecular_function	FAD binding
F	0106312	molecular_function	methylenetetrahydrofolate reductase (NADH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue FAD A 300

Chain	Residue
A	THR57
A	ALA148
A	TYR150
A	HIS154
A	GLU156
A	ALA157
A	ASP163
A	ASN166
A	ARG169
A	LYS170
A	ILE179
A	TYR58
A	TYR273
A	ACY302
A	HOH405
A	HIS86
A	LEU115
A	ARG116
A	GLY117
A	ASP118
A	TYR129
A	ALA130

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 301

Chain	Residue
A	ALA141
A	ASP142
A	HOH401
A	HOH407
C	ASP142

site_id	AC3
Number of Residues	3
Details	binding site for residue ACY A 302

Chain	Residue
A	GLU26
A	TYR273
A	FAD300

site_id	AC4
Number of Residues	2
Details	binding site for residue EDO A 303

Chain	Residue
A	TRP105
C	ARG138

site_id	AC5
Number of Residues	22
Details	binding site for residue FAD B 300

Chain	Residue
B	THR57
B	TYR58
B	HIS86
B	LEU115
B	ARG116
B	GLY117
B	ASP118
B	TYR129
B	ALA130
B	ALA148
B	TYR150
B	HIS154
B	GLU156
B	ALA157
B	ASP163
B	ASN166
B	ARG169
B	LYS170
B	TYR273
B	ACY302
B	HOH401
B	HOH402

site_id	AC6
Number of Residues	2
Details	binding site for residue SO4 B 301

Chain	Residue
B	ASP142
B	ASP144

site_id	AC7
Number of Residues	4
Details	binding site for residue ACY B 302

Chain	Residue
B	GLU26
B	GLN181
B	TYR273
B	FAD300

site_id	AC8
Number of Residues	5
Details	binding site for residue FMT B 303

Chain	Residue
B	SER24
B	LYS52
B	HIS177
B	VAL206
B	ASP269

site_id	AC9
Number of Residues	24
Details	binding site for residue FAD C 300

Chain	Residue
C	THR57
C	TYR58
C	ALA60
C	HIS86
C	THR88
C	LEU115
C	ARG116
C	GLY117
C	ASP118
C	TYR129
C	ALA130
C	ALA148
C	TYR150
C	HIS154
C	ALA157
C	ASP163
C	ASN166
C	ARG169
C	LYS170
C	ILE179
C	TYR273
C	ACY303
C	HOH403
C	HOH404

site_id	AD1
Number of Residues	6
Details	binding site for residue FMT C 301

Chain	Residue
C	SER24
C	LYS52
C	HIS177
C	VAL206
C	ASP269
C	PHE270

site_id	AD2
Number of Residues	3
Details	binding site for residue FMT C 302

Chain	Residue
C	GLU26
C	LEU275
C	HOH401

site_id	AD3
Number of Residues	4
Details	binding site for residue ACY C 303

Chain	Residue
C	GLN181
C	FAD300
C	HOH401
C	GLU26

site_id	AD4
Number of Residues	23
Details	binding site for residue FAD D 300

Chain	Residue
D	THR57
D	TYR58
D	HIS86
D	LEU115
D	ARG116
D	GLY117
D	ASP118
D	TYR129
D	ALA130
D	ALA148
D	TYR150
D	HIS154
D	GLU156
D	ALA157
D	ASP163
D	ASN166
D	ARG169
D	LYS170
D	ILE179
D	TYR273
D	ACY303
D	HOH404
D	HOH405

site_id	AD5
Number of Residues	2
Details	binding site for residue ACY D 301

Chain	Residue
D	ASP142
D	ASP144

site_id	AD6
Number of Residues	4
Details	binding site for residue ACY D 302

Chain	Residue
D	ARG102
D	ASP106
D	VAL140
E	LYS98

site_id	AD7
Number of Residues	3
Details	binding site for residue ACY D 303

Chain	Residue
D	GLU26
D	TYR273
D	FAD300

site_id	AD8
Number of Residues	4
Details	binding site for residue FMT D 304

Chain	Residue
D	SER24
D	LYS52
D	HIS177
D	ASP269

site_id	AD9
Number of Residues	25
Details	binding site for residue FAD E 300

Chain	Residue
D	GLU95
E	THR57
E	TYR58
E	HIS86
E	THR88
E	LEU115
E	ARG116
E	GLY117
E	ASP118
E	TYR129
E	ALA130
E	ALA148
E	TYR150
E	HIS154
E	GLU156
E	ALA157
E	ASP163
E	ASN166
E	ARG169
E	LYS170
E	ILE179
E	TYR273
E	ACY301
E	HOH401
E	HOH407

site_id	AE1
Number of Residues	2
Details	binding site for residue ACY E 301

Chain	Residue
E	GLU26
E	FAD300

site_id	AE2
Number of Residues	26
Details	binding site for residue FAD F 300

Chain	Residue
F	THR57
F	TYR58
F	ALA60
F	HIS86
F	THR88
F	LEU115
F	ARG116
F	GLY117
F	ASP118
F	TYR129
F	ALA130
F	ALA148
F	TYR150
F	HIS154
F	GLU156
F	ALA157
F	ASP163
F	ASN166
F	ARG169
F	LYS170
F	ILE179
F	TYR273
F	ACY301
F	HOH402
F	HOH405
F	HOH407

site_id	AE3
Number of Residues	3
Details	binding site for residue ACY F 301

Chain	Residue
F	GLU26
F	TYR273
F	FAD300

site_id	AE4
Number of Residues	2
Details	binding site for residue ACY F 302

Chain	Residue
F	ARG138
F	ASP142

site_id	AE5
Number of Residues	6
Details	binding site for residue EDO F 303

Chain	Residue
F	ASN22
F	SER24
F	LYS52
F	PHE53
F	HIS177
F	ASP269

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P0AEZ1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	107
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AEZ1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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