6PEY

MTHFR with mutation Asp120Ala

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
B	0004489	molecular_function	methylenetetrahydrofolate reductase (NAD(P)H) activity
B	0005829	cellular_component	cytosol
B	0006555	biological_process	methionine metabolic 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	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	17
Details	binding site for residue FAD A 401

Chain	Residue
A	THR59
A	TYR152
A	HIS156
A	GLU158
A	ALA159
A	ASP165
A	ASN168
A	LYS172
A	TYR275
A	TYR60
A	GLY61
A	HIS88
A	LEU117
A	ARG118
A	TYR131
A	ALA132
A	ALA150

---

site_id	AC2
Number of Residues	20
Details	binding site for residue FAD B 401

Chain	Residue
B	THR59
B	TYR60
B	ALA62
B	HIS88
B	LEU117
B	ARG118
B	GLY119
B	TYR131
B	ALA132
B	ALA150
B	TYR152
B	HIS156
B	GLU158
B	ALA159
B	ASP165
B	ASN168
B	ARG171
B	LYS172
B	GLN183
B	TYR275

---

site_id	AC3
Number of Residues	18
Details	binding site for residue FAD C 401

Chain	Residue
C	THR59
C	TYR60
C	HIS88
C	LEU117
C	ARG118
C	TYR131
C	ALA132
C	ALA150
C	TYR152
C	HIS156
C	GLU158
C	ALA159
C	ASP165
C	ASN168
C	LYS172
C	ILE181
C	GLN183
C	TYR275

---

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
B	GLU28
C	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
B	THR59
B	ALA159
B	GLN183
C	THR59
C	ALA159
C	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
B	ARG171
B	LYS172
C	TYR60
C	HIS88
C	ARG118
C	GLY119
C	ALA132
C	TYR152
C	HIS156
C	ASN168
C	ARG171
C	LYS172
A	ALA132
A	TYR152
A	HIS156
A	ASN168
A	ARG171
A	LYS172
B	TYR60
B	HIS88
B	ARG118
B	GLY119
B	ALA132
B	TYR152
B	HIS156
B	ASN168
A	GLY119
A	TYR60
A	HIS88
A	ARG118

---

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	ALA120
B	ALA62
B	ALA120
C	ALA62
C	ALA120

---

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
B	ASP165
C	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
B	GLN219
C	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
B	ARG279
C	ARG279

---

Catalytic Information from CSA

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	ALA120	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	ALA120	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	ALA120	electrostatic stabiliser, hydrogen bond acceptor
C	PHE223	steric locator
C	HIS273	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay

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