1AEQ
VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2-ETHYLIMIDAZOLE)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 295 |
| Chain | Residue |
| A | MET172 |
| A | ALA174 |
| A | HIS175 |
| A | LEU177 |
| A | GLY178 |
| A | LYS179 |
| A | THR180 |
| A | HIS181 |
| A | ASN184 |
| A | SER185 |
| A | HOH302 |
| A | HOH311 |
| A | HOH313 |
| A | HOH314 |
| A | PRO44 |
| A | VAL47 |
| A | ARG48 |
| A | TRP51 |
| A | PRO145 |
| A | ASP146 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2EZ A 296 |
| Chain | Residue |
| A | HIS175 |
| A | THR180 |
| A | MET230 |
| A | MET231 |
| A | LEU232 |
| A | ASP235 |
| A | HOH405 |
| site_id | AVE |
| Number of Residues | 3 |
| Details | REMOVAL OF TRP 191 FORMS AN INTERNAL CAVITY BELOW THE HEME RELATIVE TO THE ACTIVE SITE. |
| Chain | Residue |
| A | ARG48 |
| A | TRP51 |
| A | HIS52 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10722697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11170452","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2169873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6092361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8384877","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8673607","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| A | ARG48 | |
| A | HIS52 | |
| A | ASN82 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 709 |
| Chain | Residue | Details |
| A | ARG48 | electrostatic stabiliser |
| A | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLY191 | single electron acceptor, single electron donor |
