Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue MES A 501 |
| Chain | Residue |
| A | ASN118 |
| A | ASN121 |
| A | GLY132 |
| A | SER133 |
| A | GLY134 |
| A | LEU135 |
| A | TRP136 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | GLU461 |
| A | ASP475 |
| A | GLU452 |
| A | SER454 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue MES B 501 |
| Chain | Residue |
| B | ASN118 |
| B | ASN121 |
| B | TYR130 |
| B | GLY132 |
| B | SER133 |
| B | GLY134 |
| B | LEU135 |
| B | TRP136 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue MES C 501 |
| Chain | Residue |
| C | ASN118 |
| C | ASN121 |
| C | GLY132 |
| C | SER133 |
| C | GLY134 |
| C | LEU135 |
| C | TRP136 |
| C | SER137 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 502 |
| Chain | Residue |
| C | GLU452 |
| C | SER454 |
| C | GLU461 |
| C | ASP475 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue MES D 501 |
| Chain | Residue |
| D | ASN118 |
| D | ASN121 |
| D | GLY132 |
| D | SER133 |
| D | GLY134 |
| D | LEU135 |
| D | TRP136 |
| D | SER137 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 502 |
| Chain | Residue |
| D | GLU452 |
| D | SER454 |
| D | GLU461 |
| D | ASP475 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MES E 501 |
| Chain | Residue |
| E | ASN118 |
| E | ASN121 |
| E | SER133 |
| E | GLY134 |
| E | TRP136 |
| E | SER137 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CA E 502 |
| Chain | Residue |
| E | GLU452 |
| E | SER454 |
| E | GLU461 |
| E | ASP475 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue MES F 501 |
| Chain | Residue |
| F | ASN118 |
| F | ASN121 |
| F | GLY132 |
| F | SER133 |
| F | GLY134 |
| F | LEU135 |
| F | TRP136 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CA F 502 |
| Chain | Residue |
| F | GLU452 |
| F | SER454 |
| F | GLU461 |
| F | ASP475 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue MES G 501 |
| Chain | Residue |
| G | ASN118 |
| G | ASN121 |
| G | GLY132 |
| G | SER133 |
| G | GLY134 |
| G | LEU135 |
| G | TRP136 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MES H 501 |
| Chain | Residue |
| H | ASN118 |
| H | ASN121 |
| H | TYR130 |
| H | GLY134 |
| H | TRP136 |
| H | SER137 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CA H 502 |
| Chain | Residue |
| H | GLU452 |
| H | SER454 |
| H | GLU461 |
| H | ASP475 |
Functional Information from PROSITE/UniProt
| site_id | PS00023 |
| Number of Residues | 42 |
| Details | FN2_1 Fibronectin type-II collagen-binding domain signature. CafPFkFenkwyadCtsagrsdgwlWCgtttDYdtdklFgYC |
| Chain | Residue | Details |
| A | CYS168-CYS209 | |
| site_id | PS00615 |
| Number of Residues | 25 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVslnpgknak...WENLECvqklg.YIC |
| Chain | Residue | Details |
| A | CYS316-CYS340 | |
| A | CYS463-CYS486 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN104 | |
| E | ASN344 | |
| F | ASN104 | |
| F | ASN344 | |
| G | ASN104 | |
| G | ASN344 | |
| H | ASN104 | |
| H | ASN344 | |
| A | ASN344 | |
| B | ASN104 | |
| B | ASN344 | |
| C | ASN104 | |
| C | ASN344 | |
| D | ASN104 | |
| D | ASN344 | |
| E | ASN104 | |
