Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | HIS202 |
A | HIS348 |
A | HIS352 |
A | OLA402 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue OLA A 402 |
Chain | Residue |
A | TYR321 |
A | ALA325 |
A | TYR328 |
A | HIS348 |
A | PHE351 |
A | PHE354 |
A | ZN401 |
A | ASP219 |
A | TYR220 |
A | ILE223 |
A | LEU226 |
A | PHE282 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue OLB A 403 |
Chain | Residue |
A | SER230 |
A | GLY289 |
A | LEU314 |
A | MET315 |
A | TYR321 |
A | HIS362 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue OLB A 404 |
Chain | Residue |
A | GLY163 |
A | ILE164 |
A | MET167 |
A | PHE168 |
A | ARG169 |
A | PRO170 |
A | ASN171 |
A | LYS181 |
A | GLY276 |
A | ILE322 |
A | OLB407 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue OLB A 405 |
Chain | Residue |
A | VAL157 |
A | PHE158 |
A | CYS161 |
A | ILE164 |
A | PHE165 |
A | PHE168 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue OLB A 406 |
Chain | Residue |
A | GLN179 |
A | LEU189 |
A | VAL232 |
A | TYR240 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue OLB A 407 |
Chain | Residue |
A | ASN171 |
A | PRO272 |
A | GLN273 |
A | GLY276 |
A | ARG331 |
A | ARG335 |
A | OLB404 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue GD A 408 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue GD A 409 |
Chain | Residue |
A | GLU209 |
A | DO3411 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue DO3 A 410 |
Chain | Residue |
A | VAL105 |
A | GD408 |
A | HOH504 |
H | GD302 |
H | DO3303 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue DO3 A 411 |
Chain | Residue |
A | GLU209 |
A | ARG213 |
A | GD409 |
site_id | AD3 |
Number of Residues | 11 |
Details | binding site for residue OLB H 301 |
Chain | Residue |
A | SER131 |
A | PHE132 |
A | ARG133 |
A | PHE136 |
A | GLY301 |
A | PHE302 |
A | LEU303 |
H | ASN167 |
H | HIS169 |
H | ASN170 |
H | GLY207 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue GD H 302 |
Chain | Residue |
A | DO3410 |
H | DO3303 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue DO3 H 303 |
Chain | Residue |
A | DO3410 |
H | ASN54 |
H | SER55 |
H | GD302 |
Functional Information from PROSITE/UniProt
site_id | PS00213 |
Number of Residues | 12 |
Details | LIPOCALIN Lipocalin signature. GGS..EFEGRWRVI |
Chain | Residue | Details |
A | GLY-4-ILE106 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN148-PHE168 | |
Chain | Residue | Details |
A | ARG169-LYS181 | |
A | LEU235-PRO245 | |
A | HIS295-GLY309 | |
A | GLN370-LEU386 | |
Chain | Residue | Details |
A | VAL182-HIS202 | |
Chain | Residue | Details |
A | THR203-ARG213 | |
A | ASP267-GLN273 | |
A | ARG331-HIS348 | |
Chain | Residue | Details |
A | LEU214-TRP234 | |
Chain | Residue | Details |
A | CYS246-TRP266 | |
Chain | Residue | Details |
A | TYR274-LEU294 | |
Chain | Residue | Details |
A | GLN310-ALA330 | |
Chain | Residue | Details |
A | GLN349-LEU369 | |
Chain | Residue | Details |
A | HIS202 | |
A | HIS348 | |
A | HIS352 | |