Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0009374 | molecular_function | biotin binding |
B | 0005576 | cellular_component | extracellular region |
B | 0009374 | molecular_function | biotin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 402 |
Chain | Residue |
A | SER71 |
A | HOH429 |
A | HOH503 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT A 403 |
Chain | Residue |
A | TRP68 |
A | THR75 |
A | HOH426 |
A | HOH429 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 405 |
Chain | Residue |
A | ARG56 |
B | HOH63 |
B | HOH73 |
B | HIS267 |
A | HIS54 |
A | LYS55 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 406 |
Chain | Residue |
A | SER105 |
A | TYR106 |
B | FMT413 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 409 |
Chain | Residue |
A | VAL101 |
A | ASN102 |
A | TYR106 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 412 |
Chain | Residue |
A | LYS88 |
A | THR119 |
A | ARG120 |
A | HOH430 |
B | LYS209 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT A 415 |
Chain | Residue |
A | GLU28 |
A | ARG85 |
B | THR230 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 401 |
Chain | Residue |
B | HOH58 |
B | HOH62 |
B | HOH81 |
B | ALA238 |
B | SER271 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 404 |
Chain | Residue |
B | HOH31 |
B | HOH58 |
B | TRP268 |
B | THR275 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 407 |
Chain | Residue |
A | GLN59 |
A | PHE82 |
A | ILE83 |
B | HOH101 |
B | ASP303 |
B | ILE304 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 408 |
Chain | Residue |
A | HIS67 |
A | HOH456 |
A | HOH459 |
B | HIS254 |
B | LYS255 |
B | ARG256 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT B 410 |
Chain | Residue |
A | ALA36 |
B | THR232 |
B | LEU246 |
B | PRO248 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 411 |
Chain | Residue |
A | ASP103 |
A | ILE104 |
B | GLN259 |
B | PHE282 |
B | ILE283 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT B 413 |
Chain | Residue |
A | SER105 |
A | TYR106 |
A | TRP108 |
A | FMT406 |
B | HOH60 |
B | HOH77 |
B | VAL237 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT B 414 |
Chain | Residue |
B | HOH157 |
B | VAL301 |
B | ASN302 |
B | TYR306 |
B | LYS309 |
Functional Information from PROSITE/UniProt
site_id | PS00577 |
Number of Residues | 15 |
Details | AVIDIN_1 Avidin-like domain signature. YdwKAtrVGyNnFTR |
Chain | Residue | Details |
A | TYR106-ARG120 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN12 | |
B | TYR233 | |
B | THR235 | |
B | ALA239 | |
B | SER271 | |
B | ASN316 | |
A | SER16 | |
A | TYR33 | |
A | THR35 | |
A | ALA39 | |
A | SER71 | |
A | ASN116 | |
B | ASN212 | |
B | SER216 | |
Chain | Residue | Details |
A | ASN43 | |
A | ASN117 | |
B | ASN243 | |
B | ASN317 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN69 | |
B | ASN269 | |