1B5T
ESCHERICHIA 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 | 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 | 2 |
Details | BINDING SITE FOR RESIDUE HG A 501 |
Chain | Residue |
A | CYS91 |
A | MET130 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE HG B 501 |
Chain | Residue |
B | CYS91 |
B | ILE92 |
B | MET130 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE HG C 501 |
Chain | Residue |
C | CYS91 |
C | ILE92 |
C | ARG118 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FAD A 395 |
Chain | Residue |
A | TYR60 |
A | HIS88 |
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 | ASN168 |
A | ARG171 |
A | LYS172 |
A | TYR275 |
A | HOH606 |
A | HOH658 |
A | HOH659 |
A | HOH680 |
A | THR59 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FAD B 396 |
Chain | Residue |
B | THR59 |
B | TYR60 |
B | HIS88 |
B | THR90 |
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 | TYR275 |
B | HOH608 |
B | HOH687 |
B | HOH692 |
B | HOH696 |
B | HOH703 |
site_id | AC6 |
Number of Residues | 22 |
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 | ALA150 |
C | TYR152 |
C | HIS156 |
C | GLU158 |
C | ALA159 |
C | ASP165 |
C | ASN168 |
C | ARG171 |
C | LYS172 |
C | ILE181 |
C | TYR275 |
C | HOH663 |
C | HOH688 |
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 |
A | TYR60 | |
A | LYS172 | |
B | TYR60 | |
B | HIS88 | |
B | ARG118 | |
B | GLY119 | |
B | ALA132 | |
B | TYR152 | |
B | HIS156 | |
B | ASN168 | |
B | ARG171 | |
A | HIS88 | |
B | LYS172 | |
C | TYR60 | |
C | HIS88 | |
C | ARG118 | |
C | GLY119 | |
C | ALA132 | |
C | TYR152 | |
C | HIS156 | |
C | ASN168 | |
C | ARG171 | |
A | ARG118 | |
C | 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 | |
B | ALA62 | |
B | ASP120 | |
C | ALA62 | |
C | 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 | |
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 | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 11371182 |
Chain | Residue | Details |
A | GLU28 | |
A | ASP120 |
site_id | CSA2 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 11371182 |
Chain | Residue | Details |
B | GLU28 | |
B | ASP120 |
site_id | CSA3 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 11371182 |
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 |