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
Chain | Residue | Details |
A | HIS173 | |
A | HIS177 | |
A | HIS204 | |
A | HIS324 | |
A | HIS328 | |
A | HIS364 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN449 | |