Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0038023 | molecular_function | signaling receptor activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0090729 | molecular_function | toxin activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0038023 | molecular_function | signaling receptor activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0090729 | molecular_function | toxin activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 501 |
Chain | Residue |
A | GLU98 |
C | CGU426 |
C | CGU430 |
C | HOH1006 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 502 |
Chain | Residue |
B | HOH804 |
C | CGU408 |
C | CGU427 |
C | CGU430 |
C | HOH807 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA C 503 |
Chain | Residue |
C | CGU408 |
C | CGU417 |
C | CGU427 |
C | CGU430 |
C | HOH803 |
C | HOH805 |
C | HOH810 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 504 |
Chain | Residue |
C | TYR401 |
C | ASN402 |
C | CGU407 |
C | CGU408 |
C | CGU417 |
C | CGU427 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 505 |
Chain | Residue |
C | TYR401 |
C | CGU407 |
C | CGU417 |
C | CGU421 |
C | HOH808 |
C | HOH816 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 506 |
Chain | Residue |
C | CGU421 |
C | HOH646 |
C | HOH813 |
C | HOH817 |
C | HOH847 |
C | HOH1011 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 507 |
Chain | Residue |
C | CGU415 |
C | CGU420 |
C | HOH821 |
C | HOH826 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 508 |
Chain | Residue |
C | CGU436 |
C | CGU440 |
C | HOH802 |
C | HOH806 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 511 |
Chain | Residue |
A | SER41 |
A | GLU43 |
A | GLU47 |
A | GLU128 |
A | HOH809 |
A | HOH837 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 512 |
Chain | Residue |
B | SER241 |
B | GLN243 |
B | GLU247 |
B | GLU320 |
B | HOH818 |
B | HOH820 |
Functional Information from PROSITE/UniProt
site_id | PS00011 |
Number of Residues | 26 |
Details | GLA_1 Vitamin K-dependent carboxylation domain. EckEEkCsfeearEvfentektte.FW |
Chain | Residue | Details |
C | CGU417-TRP442 | |
site_id | PS00615 |
Number of Residues | 24 |
Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVyfkstnnk....WRSRACrmmaq.FVC |
Chain | Residue | Details |
B | CYS296-CYS319 | |
A | CYS102-CYS127 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | SER241 | |
B | GLN243 | |
B | GLU247 | |
B | GLU320 | |
Chain | Residue | Details |
A | SER41 | |
A | GLU43 | |
A | GLU47 | |
A | GLU128 | |