1ZP4
Glu28Gln mutant of E. coli Methylenetetrahydrofolate Reductase (oxidized) complex 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 |
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 998 |
Chain | Residue |
A | ARG230 |
A | PRO232 |
A | ALA233 |
A | TRP234 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 999 |
Chain | Residue |
C | ARG279 |
C | ALA280 |
C | GLU281 |
C | HOH571 |
C | HOH899 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE C2F A 995 |
Chain | Residue |
A | GLN28 |
A | ASP120 |
A | GLN183 |
A | GLN219 |
A | ALA220 |
A | PHE223 |
A | THR227 |
A | TYR275 |
A | LEU277 |
A | ARG279 |
A | FAD395 |
A | HOH606 |
A | HOH614 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE C2F B 996 |
Chain | Residue |
B | GLN28 |
B | ASP120 |
B | GLN183 |
B | GLN219 |
B | PHE223 |
B | THR227 |
B | TYR275 |
B | LEU277 |
B | ARG279 |
B | FAD396 |
B | HOH406 |
B | HOH556 |
B | HOH563 |
B | HOH761 |
B | HOH838 |
B | HOH839 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE C2F C 997 |
Chain | Residue |
C | GLN28 |
C | ASP120 |
C | GLN183 |
C | GLN219 |
C | ALA220 |
C | PHE223 |
C | THR227 |
C | TYR275 |
C | LEU277 |
C | FAD397 |
C | HOH455 |
C | HOH593 |
C | HOH603 |
C | HOH750 |
C | HOH866 |
C | HOH901 |
site_id | AC6 |
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 | ILE181 |
A | TYR275 |
A | HOH513 |
A | HOH516 |
A | HOH780 |
A | HOH903 |
A | C2F995 |
site_id | AC7 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD B 396 |
Chain | Residue |
B | LYS172 |
B | ILE181 |
B | TYR275 |
B | HOH406 |
B | HOH413 |
B | HOH435 |
B | HOH497 |
B | HOH543 |
B | HOH904 |
B | C2F996 |
B | THR59 |
B | TYR60 |
B | ALA62 |
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 |
site_id | AC8 |
Number of Residues | 29 |
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 | HOH405 |
C | HOH411 |
C | HOH422 |
C | HOH455 |
C | HOH488 |
C | HOH724 |
C | HOH905 |
C | C2F997 |
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 | |
B | GLN28 | |
C | 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 | |
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 | 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 | 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 | GLN28 | 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 | GLN28 | 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 |