2P4T
Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP A 157 |
Chain | Residue |
A | LYS32 |
A | HOH145 |
A | HOH146 |
A | HOH146 |
A | HOH146 |
A | HOH147 |
A | HOH149 |
A | HOH149 |
A | HOH151 |
A | HOH152 |
A | ALA36 |
A | VAL66 |
A | HIS67 |
A | ILE68 |
A | ILE68 |
A | TYR69 |
A | HOH144 |
A | HOH145 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17473013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18052202","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2P4T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RK2","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18052202","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RK1","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1vie |
Chain | Residue | Details |
A | ILE68 | |
A | LYS32 | |
A | TYR69 | |
A | HIS67 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 752 |
Chain | Residue | Details |
A | LYS32 | electrostatic stabiliser |
A | HIS67 | electrostatic stabiliser |
A | ILE68 | electrostatic stabiliser |
A | TYR69 | electrostatic stabiliser |