5IZQ
Crystal structure of human folate receptor alpha in complex with novel antifolate AGF183
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005542 | molecular_function | folic acid binding |
| A | 0061714 | molecular_function | folic acid receptor activity |
| A | 1904447 | biological_process | folate import across plasma membrane |
| B | 0005542 | molecular_function | folic acid binding |
| B | 0061714 | molecular_function | folic acid receptor activity |
| B | 1904447 | biological_process | folate import across plasma membrane |
| C | 0005542 | molecular_function | folic acid binding |
| C | 0061714 | molecular_function | folic acid receptor activity |
| C | 1904447 | biological_process | folate import across plasma membrane |
| D | 0005542 | molecular_function | folic acid binding |
| D | 0061714 | molecular_function | folic acid receptor activity |
| D | 1904447 | biological_process | folate import across plasma membrane |
| E | 0005542 | molecular_function | folic acid binding |
| E | 0061714 | molecular_function | folic acid receptor activity |
| E | 1904447 | biological_process | folate import across plasma membrane |
| F | 0005542 | molecular_function | folic acid binding |
| F | 0061714 | molecular_function | folic acid receptor activity |
| F | 1904447 | biological_process | folate import across plasma membrane |
| G | 0005542 | molecular_function | folic acid binding |
| G | 0061714 | molecular_function | folic acid receptor activity |
| G | 1904447 | biological_process | folate import across plasma membrane |
| H | 0005542 | molecular_function | folic acid binding |
| H | 0061714 | molecular_function | folic acid receptor activity |
| H | 1904447 | biological_process | folate import across plasma membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 83A A 300 |
| Chain | Residue |
| A | ASP81 |
| A | GLY137 |
| A | TRP138 |
| A | TRP140 |
| A | TRP171 |
| A | SER174 |
| A | TYR175 |
| A | TYR85 |
| A | GLN100 |
| A | TRP102 |
| A | ARG103 |
| A | ARG106 |
| A | TRP134 |
| A | HIS135 |
| A | LYS136 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 83A B 300 |
| Chain | Residue |
| B | TYR60 |
| B | ASP81 |
| B | TRP102 |
| B | ARG103 |
| B | ARG106 |
| B | TRP134 |
| B | HIS135 |
| B | LYS136 |
| B | GLY137 |
| B | TRP138 |
| B | TRP140 |
| B | TRP171 |
| B | SER174 |
| B | TYR175 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue 83A C 300 |
| Chain | Residue |
| C | ASP81 |
| C | TYR85 |
| C | SER101 |
| C | TRP102 |
| C | ARG103 |
| C | ARG106 |
| C | TRP134 |
| C | HIS135 |
| C | LYS136 |
| C | GLY137 |
| C | TRP138 |
| C | TRP140 |
| C | TRP171 |
| C | SER174 |
| D | LYS30 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue 83A E 300 |
| Chain | Residue |
| E | ASP81 |
| E | ARG103 |
| E | ARG106 |
| E | TRP134 |
| E | HIS135 |
| E | LYS136 |
| E | GLY137 |
| E | TRP138 |
| E | TRP140 |
| E | TRP171 |
| E | SER174 |
| E | TYR175 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue 83A F 300 |
| Chain | Residue |
| F | TYR60 |
| F | ASP81 |
| F | TYR85 |
| F | SER101 |
| F | TRP102 |
| F | ARG103 |
| F | ARG106 |
| F | TRP134 |
| F | HIS135 |
| F | LYS136 |
| F | GLY137 |
| F | TRP138 |
| F | TRP140 |
| F | TRP171 |
| F | SER174 |
| F | TYR175 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue 83A G 300 |
| Chain | Residue |
| G | ASP81 |
| G | TYR85 |
| G | SER101 |
| G | TRP102 |
| G | ARG103 |
| G | ARG106 |
| G | TRP134 |
| G | HIS135 |
| G | LYS136 |
| G | GLY137 |
| G | TRP138 |
| G | TRP140 |
| G | TRP171 |
| G | SER174 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue 83A H 300 |
| Chain | Residue |
| H | TYR175 |
| H | ASP81 |
| H | TYR85 |
| H | TRP102 |
| H | ARG103 |
| H | ARG106 |
| H | TRP134 |
| H | HIS135 |
| H | LYS136 |
| H | GLY137 |
| H | TRP138 |
| H | TRP140 |
| H | TRP171 |
| H | SER174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23851396","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Lipidation: {"description":"GPI-anchor amidated serine","evidences":[{"source":"PubMed","id":"17566972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7578066","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23851396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23934049","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23851396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23934049","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
