Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0007155 | biological_process | cell adhesion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | ARG333 |
| A | ASN335 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OLC A 502 |
| Chain | Residue |
| A | ILE389 |
| A | OLC505 |
| A | OLC514 |
| A | GLN218 |
| A | SER219 |
| A | GLY225 |
| A | SER226 |
| A | TYR250 |
| A | VAL377 |
| A | TYR379 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OLC A 503 |
| Chain | Residue |
| A | GLY273 |
| A | GLY292 |
| A | GLY293 |
| A | VAL304 |
| A | ARG309 |
| A | ASN328 |
| A | TYR354 |
| A | OLC509 |
| A | HOH727 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLB A 504 |
| Chain | Residue |
| A | TYR235 |
| A | GLN263 |
| A | TYR274 |
| A | OLC506 |
| A | OLC509 |
| A | OLC511 |
| A | OLC513 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE OLC A 505 |
| Chain | Residue |
| A | VAL215 |
| A | SER226 |
| A | ALA248 |
| A | TYR379 |
| A | MET387 |
| A | OLC502 |
| A | OLB508 |
| A | OLC512 |
| A | OLC514 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OLC A 506 |
| Chain | Residue |
| A | PHE234 |
| A | TYR235 |
| A | LEU338 |
| A | PRO339 |
| A | SER340 |
| A | OLB504 |
| A | OLC511 |
| A | OLC513 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OLC A 507 |
| Chain | Residue |
| A | ARG297 |
| A | ASP298 |
| A | TYR299 |
| A | TYR337 |
| A | LEU338 |
| A | LEU344 |
| A | ALA346 |
| A | VAL377 |
| A | OLC512 |
| A | HOH753 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLB A 508 |
| Chain | Residue |
| A | SER219 |
| A | GLY220 |
| A | ASN221 |
| A | TYR403 |
| A | TYR409 |
| A | OLC505 |
| A | HOH759 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OLC A 509 |
| Chain | Residue |
| A | ARG309 |
| A | MET310 |
| A | GLY312 |
| A | TRP313 |
| A | ARG325 |
| A | PHE330 |
| A | TYR354 |
| A | OLC503 |
| A | OLB504 |
| A | OLB510 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLB A 510 |
| Chain | Residue |
| A | VAL304 |
| A | PHE330 |
| A | ILE332 |
| A | GLN352 |
| A | TYR354 |
| A | ASN369 |
| A | OLC509 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OLC A 511 |
| Chain | Residue |
| A | LEU232 |
| A | PRO233 |
| A | PHE234 |
| A | GLY244 |
| A | ALA261 |
| A | ILE278 |
| A | SER340 |
| A | TYR341 |
| A | LEU344 |
| A | OLB504 |
| A | OLC506 |
| A | HOH698 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 512 |
| Chain | Residue |
| A | TYR341 |
| A | VAL377 |
| A | OLC505 |
| A | OLC507 |
| A | OLC514 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OLC A 513 |
| Chain | Residue |
| A | GLN263 |
| A | LEU267 |
| A | LEU272 |
| A | TYR274 |
| A | OLB504 |
| A | OLC506 |
| A | HOH730 |
| A | TYR235 |
| A | SER237 |
| A | MET240 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OLC A 514 |
| Chain | Residue |
| A | HIS209 |
| A | PHE230 |
| A | ALA257 |
| A | OLC502 |
| A | OLC505 |
| A | OLC512 |
| A | HOH759 |
Functional Information from PROSITE/UniProt
| site_id | PS00180 |
| Number of Residues | 19 |
| Details | GLNA_1 Glutamine synthetase signature 1. FDGSSldfllpfyDSEkmL |
| Chain | Residue | Details |
| A | PHE223-LEU241 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 201 |
| Details | Region: {"description":"Inverse autotransporter","evidences":[{"source":"PubMed","id":"22658748","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Region: {"description":"Signature sequence for beta-barrel assembly machinery (BAM), which recognizes the unfolded beta-barrel in the periplasm","evidences":[{"source":"PubMed","id":"22658748","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Region: {"description":"Minimum linker residues necessary for formation of a heat-modifiable beta-barrel","evidences":[{"source":"PubMed","id":"22658748","evidenceCode":"ECO:0000269"}]} |