3FSU
Crystal Structure of Escherichia coli Methylenetetrahydrofolate Reductase Double Mutant Phe223LeuGlu28Gln complexed with methyltetrahydrofolate
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 |
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 |
E | 0004489 | molecular_function | methylenetetrahydrofolate reductase (NAD(P)H) activity |
E | 0005829 | cellular_component | cytosol |
E | 0006555 | biological_process | methionine metabolic process |
E | 0009086 | biological_process | methionine biosynthetic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0032991 | cellular_component | protein-containing complex |
E | 0035999 | biological_process | tetrahydrofolate interconversion |
E | 0051087 | molecular_function | protein-folding chaperone binding |
E | 0071949 | molecular_function | FAD binding |
E | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD A 395 |
Chain | Residue |
A | THR59 |
A | TYR131 |
A | ALA132 |
A | ALA150 |
A | TYR152 |
A | HIS156 |
A | GLU158 |
A | ALA159 |
A | ASP165 |
A | ASN168 |
A | ARG171 |
A | TYR60 |
A | LYS172 |
A | ILE181 |
A | GLN183 |
A | TYR275 |
A | HOH322 |
A | HOH338 |
A | HOH364 |
A | HOH368 |
A | C2F995 |
A | ALA62 |
A | HIS88 |
A | THR90 |
A | LEU117 |
A | ARG118 |
A | GLY119 |
A | ASP120 |
site_id | AC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD C 395 |
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 | HOH341 |
C | HOH344 |
C | HOH382 |
C | HOH398 |
C | HOH426 |
C | HOH454 |
C | HOH456 |
C | HOH477 |
C | MRY5320 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FAD E 395 |
Chain | Residue |
E | THR59 |
E | TYR60 |
E | HIS88 |
E | THR90 |
E | LEU117 |
E | ARG118 |
E | GLY119 |
E | ASP120 |
E | TYR131 |
E | ALA132 |
E | ALA150 |
E | TYR152 |
E | HIS156 |
E | GLU158 |
E | ALA159 |
E | ASP165 |
E | ASN168 |
E | ARG171 |
E | LYS172 |
E | ILE181 |
E | GLN183 |
E | TYR275 |
E | HOH315 |
E | HOH350 |
E | C2F995 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE C2F A 995 |
Chain | Residue |
A | GLN28 |
A | ASP120 |
A | GLN183 |
A | SER215 |
A | GLN219 |
A | LEU223 |
A | THR227 |
A | TYR275 |
A | LEU277 |
A | ARG279 |
A | HOH364 |
A | HOH366 |
A | HOH389 |
A | FAD395 |
A | HOH406 |
A | HOH452 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE C2F E 995 |
Chain | Residue |
E | GLN28 |
E | ASP120 |
E | GLN183 |
E | SER215 |
E | GLN219 |
E | LEU223 |
E | THR227 |
E | TYR275 |
E | LEU277 |
E | ARG279 |
E | HOH336 |
E | HOH348 |
E | HOH350 |
E | HOH394 |
E | FAD395 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MRY C5320 |
Chain | Residue |
C | GLN28 |
C | GLN183 |
C | PHE184 |
C | LEU277 |
C | HOH356 |
C | HOH359 |
C | HOH360 |
C | FAD395 |
C | HOH399 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 305 |
Chain | Residue |
E | ARG230 |
E | PRO232 |
E | ALA233 |
E | TRP234 |
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 | GLN28 | |
C | GLN28 | |
E | GLN28 |
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 | |
C | THR59 | |
C | ALA159 | |
C | GLN183 | |
E | THR59 | |
E | ALA159 | |
E | 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 | |
C | TYR60 | |
C | HIS88 | |
C | ARG118 | |
C | GLY119 | |
C | ALA132 | |
C | TYR152 | |
C | HIS156 | |
C | ASN168 | |
C | ARG171 | |
A | HIS88 | |
C | LYS172 | |
E | TYR60 | |
E | HIS88 | |
E | ARG118 | |
E | GLY119 | |
E | ALA132 | |
E | TYR152 | |
E | HIS156 | |
E | ASN168 | |
E | ARG171 | |
A | ARG118 | |
E | 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 | |
C | ALA62 | |
C | ASP120 | |
E | ALA62 | |
E | 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 | |
C | ASP165 | |
E | 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 | |
C | GLN219 | |
E | 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 | |
C | ARG279 | |
E | ARG279 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b5t |
Chain | Residue | Details |
A | GLN28 | |
A | ASP120 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b5t |
Chain | Residue | Details |
C | GLN28 | |
C | ASP120 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b5t |
Chain | Residue | Details |
E | GLN28 | |
E | 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 | GLN28 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ASP120 | electrostatic stabiliser, hydrogen bond acceptor |
A | LEU223 | 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 |
C | SER26 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | GLN28 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | ASP120 | electrostatic stabiliser, hydrogen bond acceptor |
C | LEU223 | steric locator |
C | 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 |
E | SER26 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
E | GLN28 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
E | ASP120 | electrostatic stabiliser, hydrogen bond acceptor |
E | LEU223 | steric locator |
E | HIS273 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |