6ECR
The human methylenetetrahydrofolate dehydrogenase/cyclohydrolase (FolD) complexed with NADP
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | THR148 |
| A | GLN218 |
| A | CYS236 |
| A | GLY237 |
| A | ILE238 |
| A | THR279 |
| A | HOH405 |
| A | HOH408 |
| A | HOH418 |
| A | HOH442 |
| A | ARG173 |
| A | SER174 |
| A | VAL177 |
| A | HIS196 |
| A | SER197 |
| A | ALA215 |
| A | THR216 |
| A | GLY217 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | THR148 |
| B | GLY172 |
| B | ARG173 |
| B | SER174 |
| B | VAL177 |
| B | HIS196 |
| B | SER197 |
| B | ALA215 |
| B | THR216 |
| B | GLY217 |
| B | GLN218 |
| B | MET221 |
| B | CYS236 |
| B | GLY237 |
| B | ILE238 |
| B | THR279 |
| B | HOH413 |
| B | HOH414 |
| B | HOH427 |
| B | HOH438 |
| B | HOH453 |
| B | HOH463 |
| B | HOH484 |
| B | HOH494 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 302 |
| Chain | Residue |
| A | GLY160 |
| A | PRO162 |
| B | GLN23 |
| B | GLU289 |
| B | LYS292 |
| B | HOH406 |
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 |
