1ZRQ
Escherichia coli Methylenetetrahydrofolate Reductase (reduced) complexed with NADH, pH 6.0
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 | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 899 |
| Chain | Residue |
| A | ARG230 |
| A | PRO232 |
| A | ALA233 |
| A | TRP234 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 900 |
| Chain | Residue |
| A | ARG279 |
| A | ALA280 |
| A | GLU281 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| B | GLU281 |
| B | ARG279 |
| B | ALA280 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 902 |
| Chain | Residue |
| C | ARG279 |
| C | ALA280 |
| C | GLU281 |
| C | HOH663 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 395 |
| Chain | Residue |
| A | THR59 |
| A | TYR60 |
| 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 | ASN168 |
| A | ARG171 |
| A | LYS172 |
| A | TYR275 |
| A | NAI495 |
| A | HOH605 |
| A | HOH619 |
| A | HOH639 |
| A | HOH756 |
| A | HOH756 |
| site_id | AC6 |
| Number of Residues | 26 |
| 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 | NAI496 |
| B | HOH510 |
| B | HOH512 |
| B | HOH521 |
| B | HOH522 |
| B | HOH598 |
| site_id | AC7 |
| Number of Residues | 28 |
| 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 | GLN183 |
| C | TYR275 |
| C | NAI497 |
| C | HOH506 |
| C | HOH509 |
| C | HOH528 |
| C | HOH532 |
| C | HOH696 |
| C | HOH746 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NAI A 495 |
| Chain | Residue |
| A | THR227 |
| A | LEU277 |
| A | FAD395 |
| A | HOH618 |
| A | PHE30 |
| A | ARG33 |
| A | THR59 |
| A | GLN183 |
| A | PHE223 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NAI B 496 |
| Chain | Residue |
| B | PHE30 |
| B | THR59 |
| B | ASP120 |
| B | GLN183 |
| B | PHE184 |
| B | PHE223 |
| B | LEU277 |
| B | FAD396 |
| B | HOH577 |
| B | HOH620 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NAI C 497 |
| Chain | Residue |
| C | GLU28 |
| C | PHE30 |
| C | THR59 |
| C | TYR60 |
| C | GLY61 |
| C | SER64 |
| C | GLN183 |
| C | PHE223 |
| C | TYR275 |
| C | LEU277 |
| C | FAD397 |
| C | HOH617 |
| C | HOH656 |
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 | 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 |
