Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0015671 | biological_process | oxygen transport |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031404 | molecular_function | chloride ion binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 629 |
| Chain | Residue |
| A | HIS173 |
| A | HIS177 |
| A | HIS204 |
| A | CU630 |
| A | PER631 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 630 |
| Chain | Residue |
| A | HIS324 |
| A | HIS328 |
| A | HIS364 |
| A | CU629 |
| A | PER631 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 632 |
| Chain | Residue |
| A | SER507 |
| A | THR510 |
| A | ASP578 |
| A | HOH781 |
| A | HOH794 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 A 633 |
| Chain | Residue |
| A | SER47 |
| A | HIS50 |
| A | VAL329 |
| A | ALA332 |
| A | ARG333 |
| A | SER349 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PER A 631 |
| Chain | Residue |
| A | PHE49 |
| A | HIS173 |
| A | HIS177 |
| A | HIS204 |
| A | HIS324 |
| A | HIS328 |
| A | PHE360 |
| A | HIS364 |
| A | CU629 |
| A | CU630 |
| site_id | ANI |
| Number of Residues | 2 |
| Details | BINDING SITE FOR ANIONS (NITRATE AND CHLORIDE BINDING HAS BEEN OBSERVED) |
| Chain | Residue |
| A | SER47 |
| A | ARG333 |
| site_id | CAL |
| Number of Residues | 5 |
| Details | BINDING SITE FOR CALCIUM ION. THIS SITE MAY ALSO BIND SODIUM (SEE PDB ENTRY 1LLA) |
| Chain | Residue |
| A | THR510 |
| A | ASP578 |
| A | HOH781 |
| A | HOH794 |
| A | SER507 |
| site_id | CUA |
| Number of Residues | 3 |
| Details | BINDING SITE FOR COPPER A |
| Chain | Residue |
| A | HIS173 |
| A | HIS177 |
| A | HIS204 |
| site_id | CUB |
| Number of Residues | 3 |
| Details | BINDING SITE FOR COPPER B |
| Chain | Residue |
| A | HIS324 |
| A | HIS328 |
| A | HIS364 |
Functional Information from PROSITE/UniProt
| site_id | PS00209 |
| Number of Residues | 20 |
| Details | HEMOCYANIN_1 Arthropod hemocyanins / insect LSPs signature 1. YYrEDVgiNahhwhwHlvyP |
| Chain | Residue | Details |
| A | TYR162-PRO181 | |
| site_id | PS00210 |
| Number of Residues | 9 |
| Details | HEMOCYANIN_2 Arthropod hemocyanins / insect LSPs signature 2. TslRDPiFY |
| Chain | Residue | Details |
| A | THR353-TYR361 | |
| site_id | PS00498 |
| Number of Residues | 12 |
| Details | TYROSINASE_2 Tyrosinase and hemocyanins CuB-binding region signature. DPiFYnwHrfiD |
| Chain | Residue | Details |
| A | ASP357-ASP368 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8518732","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Blocked amino end (Thr); partial","evidences":[{"source":"PubMed","id":"3525550","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bt1 |
| Chain | Residue | Details |
| A | TYR320 | |
