6ECQ
The human methylenetetrahydrofolate dehydrogenase/cyclohydrolase (FolD) complexed with NADP and inhibitor LY345899
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | THR148 |
| A | GLY217 |
| A | GLN218 |
| A | CYS236 |
| A | ILE238 |
| A | ASN239 |
| A | THR279 |
| A | LUD401 |
| A | HOH512 |
| A | HOH518 |
| A | HOH528 |
| A | ARG173 |
| A | SER174 |
| A | VAL177 |
| A | HIS196 |
| A | SER197 |
| A | LEU202 |
| A | ALA215 |
| A | THR216 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue LUD A 401 |
| Chain | Residue |
| A | VAL55 |
| A | LYS56 |
| A | VAL99 |
| A | GLN100 |
| A | LEU101 |
| A | ASP125 |
| A | ILE238 |
| A | PRO272 |
| A | GLY273 |
| A | PRO277 |
| A | VAL280 |
| A | NAP301 |
| A | HOH502 |
| A | HOH528 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | THR148 |
| B | ARG173 |
| B | SER174 |
| B | HIS196 |
| B | SER197 |
| B | LEU202 |
| B | ALA215 |
| B | THR216 |
| B | GLN218 |
| B | MET221 |
| B | CYS236 |
| B | GLY237 |
| B | ILE238 |
| B | THR279 |
| B | HOH416 |
| B | HOH419 |
| B | HOH430 |
| B | HOH435 |
Functional Information from PROSITE/UniProt
| site_id | PS00766 |
| Number of Residues | 26 |
| Details | THF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. EsEVMkyItsLNeDstvhgFLVQLPL |
| Chain | Residue | Details |
| A | GLU78-LEU103 |
| site_id | PS00767 |
| Number of Residues | 9 |
| Details | THF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTV |
| Chain | Residue | Details |
| A | PRO272-VAL280 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"10828945","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10828945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DIB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10828945","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9519408","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A4I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DIG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 289 |
| Details | Region: {"description":"Methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase (D/C) domain","evidences":[{"source":"PubMed","id":"1881876","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 389 |
| Chain | Residue | Details |
| A | LYS56 | activator |
| A | GLN100 | activator |
| A | ASP125 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 458 |
| Chain | Residue | Details |
| A | SER49 | activator |
| A | LYS56 | proton shuttle (general acid/base) |
| A | GLN100 | activator |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 389 |
| Chain | Residue | Details |
| B | LYS56 | activator |
| B | GLN100 | activator |
| B | ASP125 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 458 |
| Chain | Residue | Details |
| B | SER49 | activator |
| B | LYS56 | proton shuttle (general acid/base) |
| B | GLN100 | activator |
