4U9L
Structure of a membrane protein
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 501 |
Chain | Residue |
A | HOH605 |
A | HOH606 |
A | HOH607 |
B | HOH606 |
B | HOH607 |
B | HOH609 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue OLC A 502 |
Chain | Residue |
A | PHE410 |
A | LEU411 |
A | ARG414 |
B | TYR379 |
A | LEU349 |
A | TRP352 |
A | ARG353 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue OLC A 503 |
Chain | Residue |
A | ARG345 |
A | TRP380 |
B | ARG353 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue OLC A 504 |
Chain | Residue |
A | PHE372 |
A | VAL375 |
A | LYS377 |
A | TRP380 |
B | OLC502 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue OLC B 501 |
Chain | Residue |
A | TYR379 |
B | LEU349 |
B | TRP352 |
B | ARG353 |
B | PHE410 |
B | ARG414 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue OLC B 502 |
Chain | Residue |
A | OLC504 |
B | LEU294 |
B | SER301 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 234 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB |
Chain | Residue | Details |
A | ALA284-PHE306 | |
B | LEU421-ALA443 | |
A | LEU316-LEU337 | |
A | TRP352-ASP381 | |
A | LEU386-PRO409 | |
A | LEU421-ALA443 | |
B | ALA284-PHE306 | |
B | LEU316-LEU337 | |
B | TRP352-ASP381 | |
B | LEU386-PRO409 |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 |
Chain | Residue | Details |
A | GLU307-ALA315 | |
A | GLY382-LEU385 | |
B | GLU307-ALA315 | |
B | GLY382-LEU385 |
site_id | SWS_FT_FI3 |
Number of Residues | 46 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295 |
Chain | Residue | Details |
A | ILE338-ASP351 | |
A | PHE410-ALA420 | |
B | ILE338-ASP351 | |
B | PHE410-ALA420 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N |
Chain | Residue | Details |
A | GLU275 | |
B | HIS383 | |
A | GLN304 | |
A | GLU307 | |
A | GLU311 | |
A | HIS383 | |
B | GLU275 | |
B | GLN304 | |
B | GLU307 | |
B | GLU311 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9 |
Chain | Residue | Details |
A | ASP418 | |
B | ASP418 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19798051 |
Chain | Residue | Details |
A | ALA428 | |
B | ALA428 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715 |
Chain | Residue | Details |
A | ASP432 | |
B | ASP432 |