3GD7
Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
A | 0055085 | biological_process | transmembrane transport |
B | 0005524 | molecular_function | ATP binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0022857 | molecular_function | transmembrane transporter activity |
B | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
B | 0055085 | biological_process | transmembrane transport |
C | 0005524 | molecular_function | ATP binding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0022857 | molecular_function | transmembrane transporter activity |
C | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
C | 0055085 | biological_process | transmembrane transport |
D | 0005524 | molecular_function | ATP binding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0022857 | molecular_function | transmembrane transporter activity |
D | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
D | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE B44 A 1 |
Chain | Residue |
A | HOH5 |
A | THR1252 |
A | LEU1260 |
B | PHE1296 |
B | SER1297 |
A | TYR1219 |
A | ILE1226 |
A | THR1246 |
A | GLY1247 |
A | SER1248 |
A | GLY1249 |
A | LYS1250 |
A | SER1251 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE B44 B 2 |
Chain | Residue |
A | PHE1294 |
A | PHE1296 |
B | HOH6 |
B | HOH128 |
B | HOH145 |
B | HOH189 |
B | TYR1219 |
B | ILE1226 |
B | THR1246 |
B | GLY1247 |
B | SER1248 |
B | GLY1249 |
B | LYS1250 |
B | SER1251 |
B | THR1252 |
B | LEU1260 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE B44 C 3 |
Chain | Residue |
C | HOH7 |
C | TYR1219 |
C | ILE1226 |
C | ARG1245 |
C | THR1246 |
C | GLY1247 |
C | SER1248 |
C | GLY1249 |
C | LYS1250 |
C | SER1251 |
C | THR1252 |
C | SER1255 |
D | PHE1294 |
D | PHE1296 |
D | SER1297 |
D | LYS1302 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE B44 D 4 |
Chain | Residue |
C | PHE1294 |
C | PHE1296 |
D | HOH8 |
D | TYR1219 |
D | ILE1226 |
D | THR1246 |
D | GLY1247 |
D | SER1248 |
D | GLY1249 |
D | LYS1250 |
D | SER1251 |
D | THR1252 |
D | LEU1260 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:3GD7 |
Chain | Residue | Details |
A | TYR1219 | |
B | TYR1219 | |
C | TYR1219 | |
D | TYR1219 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:3GD7 |
Chain | Residue | Details |
A | GLY1244 | |
B | GLY1244 | |
C | GLY1244 | |
D | GLY1244 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 |
Chain | Residue | Details |
A | CYS1395 | |
B | CYS1395 | |
C | CYS1395 | |
D | CYS1395 |