Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001666 | biological_process | response to hypoxia |
A | 0005344 | molecular_function | oxygen carrier activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0015671 | biological_process | oxygen transport |
A | 0019825 | molecular_function | oxygen binding |
A | 0020037 | molecular_function | heme binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0001666 | biological_process | response to hypoxia |
B | 0005344 | molecular_function | oxygen carrier activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0015671 | biological_process | oxygen transport |
B | 0019825 | molecular_function | oxygen binding |
B | 0020037 | molecular_function | heme binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0001666 | biological_process | response to hypoxia |
C | 0005344 | molecular_function | oxygen carrier activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0015671 | biological_process | oxygen transport |
C | 0019825 | molecular_function | oxygen binding |
C | 0020037 | molecular_function | heme binding |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0001666 | biological_process | response to hypoxia |
D | 0005344 | molecular_function | oxygen carrier activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0015671 | biological_process | oxygen transport |
D | 0019825 | molecular_function | oxygen binding |
D | 0020037 | molecular_function | heme binding |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM A 147 |
Chain | Residue |
A | TYR50 |
A | ILE114 |
A | CMO148 |
B | ASN100 |
A | PHE51 |
A | HIS69 |
A | LEU73 |
A | PHE97 |
A | ASN100 |
A | HIS101 |
A | ARG104 |
A | PHE111 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CMO A 148 |
Chain | Residue |
A | MET37 |
A | PHE51 |
A | HIS69 |
A | LEU73 |
A | HEM147 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HEM B 147 |
Chain | Residue |
A | ASN100 |
B | TYR50 |
B | PHE51 |
B | ARG53 |
B | HIS69 |
B | LEU73 |
B | LEU77 |
B | PHE97 |
B | HIS101 |
B | ARG104 |
B | PHE111 |
B | ILE114 |
B | CMO148 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CMO B 148 |
Chain | Residue |
B | MET37 |
B | PHE51 |
B | HIS69 |
B | LEU73 |
B | HEM147 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HEM C 147 |
Chain | Residue |
C | TYR50 |
C | PHE51 |
C | ARG53 |
C | HIS69 |
C | THR72 |
C | LEU73 |
C | LEU77 |
C | PHE97 |
C | ASN100 |
C | HIS101 |
C | ARG104 |
C | GLU110 |
C | PHE111 |
C | CMO148 |
D | ARG96 |
D | ASN100 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CMO C 148 |
Chain | Residue |
C | MET37 |
C | PHE51 |
C | HIS69 |
C | LEU73 |
C | HEM147 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE HEM D 147 |
Chain | Residue |
C | ASN100 |
D | TYR50 |
D | PHE51 |
D | ARG53 |
D | HIS69 |
D | LEU77 |
D | PHE97 |
D | HIS101 |
D | ARG104 |
D | GLU110 |
D | PHE111 |
D | ILE114 |
D | CMO148 |
D | HOH158 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CMO D 148 |
Chain | Residue |
D | MET37 |
D | HIS69 |
D | LEU73 |
D | HEM147 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: proximal binding residue |
Chain | Residue | Details |
A | HIS101 | |
B | HIS101 | |
C | HIS101 | |
D | HIS101 | |