5AO5
Endo180 D1-4, monoclinic form
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 901 |
| Chain | Residue |
| A | GLN326 |
| A | ASP328 |
| A | GLU333 |
| A | ASN348 |
| A | HOH2078 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 902 |
| Chain | Residue |
| A | HOH2092 |
| A | GLU470 |
| A | ASN472 |
| A | ASP493 |
| A | HOH2090 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 901 |
| Chain | Residue |
| B | GLN326 |
| B | ASP328 |
| B | GLU333 |
| B | ASN348 |
| B | HOH2053 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 902 |
| Chain | Residue |
| B | GLU470 |
| B | ASN472 |
| B | ASP493 |
| B | HOH2066 |
| B | HOH2067 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1512 |
| Chain | Residue |
| A | THR216 |
| A | GLN217 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1511 |
| Chain | Residue |
| B | ARG260 |
| B | ASP350 |
| B | CYS351 |
| B | ARG401 |
| B | HOH2052 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1513 |
| Chain | Residue |
| A | GLY205 |
| A | ARG206 |
| A | TYR219 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1512 |
| Chain | Residue |
| B | ARG206 |
| B | TRP212 |
| B | TYR219 |
| B | TRP225 |
Functional Information from PROSITE/UniProt
| site_id | PS00023 |
| Number of Residues | 42 |
| Details | FN2_1 Fibronectin type-II collagen-binding domain signature. CtiPFkYdnqwfhgCtstgredghlWCattqDYgkderWgFC |
| Chain | Residue | Details |
| A | CYS187-CYS228 |
| site_id | PS00615 |
| Number of Residues | 25 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CGvirtessgg...WQNRDCsialp.YVC |
| Chain | Residue | Details |
| A | CYS335-CYS359 | |
| A | CYS481-CYS504 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | Domain: {"description":"Fibronectin type-II","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 232 |
| Details | Domain: {"description":"C-type lectin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 232 |
| Details | Domain: {"description":"C-type lectin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
