Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0046872 | molecular_function | metal ion binding |
A | 0090729 | molecular_function | toxin activity |
A | 0099106 | molecular_function | ion channel regulator activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0046872 | molecular_function | metal ion binding |
B | 0090729 | molecular_function | toxin activity |
B | 0099106 | molecular_function | ion channel regulator activity |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0035821 | biological_process | modulation of process of another organism |
C | 0046872 | molecular_function | metal ion binding |
C | 0090729 | molecular_function | toxin activity |
C | 0099106 | molecular_function | ion channel regulator activity |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0035821 | biological_process | modulation of process of another organism |
D | 0046872 | molecular_function | metal ion binding |
D | 0090729 | molecular_function | toxin activity |
D | 0099106 | molecular_function | ion channel regulator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | HIS51 |
A | HIS106 |
D | HOH309 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 302 |
Chain | Residue |
B | HIS51 |
B | HIS106 |
B | HOH303 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 303 |
Chain | Residue |
B | HOH304 |
C | HIS51 |
C | HIS106 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 304 |
Chain | Residue |
D | HIS51 |
D | HIS106 |
D | HOH310 |
D | HOH328 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 305 |
Chain | Residue |
A | HIS206 |
A | HOH307 |
A | HOH308 |
C | PHE204 |
C | HIS206 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 306 |
Chain | Residue |
A | SER72 |
A | GLN73 |
A | SER127 |
A | SER128 |
A | HOH309 |
A | HOH379 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA C 307 |
Chain | Residue |
C | SER72 |
C | GLN73 |
C | SER127 |
C | HOH308 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA D 308 |
Chain | Residue |
D | SER72 |
D | GLN73 |
D | SER127 |
D | HOH313 |
Functional Information from PROSITE/UniProt
site_id | PS01009 |
Number of Residues | 11 |
Details | CRISP_1 CRISP family signature 1. GHYTQVVWykS |
Chain | Residue | Details |
A | GLY105-SER115 | |
site_id | PS01010 |
Number of Residues | 12 |
Details | CRISP_2 CRISP family signature 2. LYvCQYcPaGNI |
Chain | Residue | Details |
A | LEU131-ILE142 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR23 | |
A | SER78 | |
B | THR23 | |
B | SER78 | |
C | THR23 | |
C | SER78 | |
D | THR23 | |
D | SER78 | |