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 | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23851396 |
Chain | Residue | Details |
A | ASP81 | |
B | SER174 | |
C | ASP81 | |
C | TYR85 | |
C | TRP102 | |
C | HIS135 | |
C | SER174 | |
D | ASP81 | |
D | TYR85 | |
D | TRP102 | |
D | HIS135 | |
A | TYR85 | |
D | SER174 | |
E | ASP81 | |
E | TYR85 | |
E | TRP102 | |
E | HIS135 | |
E | SER174 | |
F | ASP81 | |
F | TYR85 | |
F | TRP102 | |
F | HIS135 | |
A | TRP102 | |
F | SER174 | |
G | ASP81 | |
G | TYR85 | |
G | TRP102 | |
G | HIS135 | |
G | SER174 | |
H | ASP81 | |
H | TYR85 | |
H | TRP102 | |
H | HIS135 | |
A | HIS135 | |
H | SER174 | |
A | SER174 | |
B | ASP81 | |
B | TYR85 | |
B | TRP102 | |
B | HIS135 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | LIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:17566972, ECO:0000269|PubMed:7578066 |
Chain | Residue | Details |
A | SER212 | |
B | SER212 | |
C | SER212 | |
D | SER212 | |
E | SER212 | |
F | SER212 | |
G | SER212 | |
H | SER212 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23851396, ECO:0000269|PubMed:23934049 |
Chain | Residue | Details |
A | ASN47 | |
B | ASN47 | |
C | ASN47 | |
D | ASN47 | |
E | ASN47 | |
F | ASN47 | |
G | ASN47 | |
H | ASN47 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:23851396, ECO:0000269|PubMed:23934049 |
Chain | Residue | Details |
A | ASN139 | |
E | ASN179 | |
F | ASN139 | |
F | ASN179 | |
G | ASN139 | |
G | ASN179 | |
H | ASN139 | |
H | ASN179 | |
A | ASN179 | |
B | ASN139 | |
B | ASN179 | |
C | ASN139 | |
C | ASN179 | |
D | ASN139 | |
D | ASN179 | |
E | ASN139 |