5FCR
MOUSE COMPLEMENT FACTOR D
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006508 | biological_process | proteolysis |
A | 0006957 | biological_process | complement activation, alternative pathway |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0009617 | biological_process | response to bacterium |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0006508 | biological_process | proteolysis |
B | 0006957 | biological_process | complement activation, alternative pathway |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0009617 | biological_process | response to bacterium |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0006508 | biological_process | proteolysis |
C | 0006957 | biological_process | complement activation, alternative pathway |
C | 0008236 | molecular_function | serine-type peptidase activity |
C | 0009617 | biological_process | response to bacterium |
D | 0004252 | molecular_function | serine-type endopeptidase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0006508 | biological_process | proteolysis |
D | 0006957 | biological_process | complement activation, alternative pathway |
D | 0008236 | molecular_function | serine-type peptidase activity |
D | 0009617 | biological_process | response to bacterium |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue EPE B 301 |
Chain | Residue |
B | HIS91 |
B | GLU100 |
B | ASP101 |
B | ASN179 |
B | SER233 |
B | TYR234 |
B | MET236 |
B | TRP237 |
B | HOH545 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
B | GLU21 |
B | ARG150 |
B | PRO152 |
B | ASP153 |
B | VAL154 |
B | HIS156 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue EPE C 301 |
Chain | Residue |
C | HIS91 |
C | GLU100 |
C | ASP101 |
C | ASN179 |
C | SER233 |
C | TYR234 |
C | MET236 |
C | TRP237 |
C | HOH432 |
C | HOH515 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 302 |
Chain | Residue |
C | ARG150 |
C | PRO152 |
C | ASP153 |
C | VAL154 |
C | HIS156 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue DMS D 301 |
Chain | Residue |
D | HIS91 |
D | TYR234 |
D | MET236 |
D | TRP237 |
D | HOH493 |
D | HOH556 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue DMS D 302 |
Chain | Residue |
D | GLU21 |
D | ARG150 |
D | PRO152 |
D | ASP153 |
D | VAL154 |
D | HIS156 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | HIS57 | |
D | HIS57 | |
D | ASP102 | |
D | SER195 | |
A | ASP102 | |
A | SER195 | |
B | HIS57 | |
B | ASP102 | |
B | SER195 | |
C | HIS57 | |
C | ASP102 | |
C | SER195 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN36 | |
D | ASN36 | |
D | ASN240 | |
D | ASN245 | |
A | ASN240 | |
A | ASN245 | |
B | ASN36 | |
B | ASN240 | |
B | ASN245 | |
C | ASN36 | |
C | ASN240 | |
C | ASN245 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944957 |
Chain | Residue | Details |
A | ASN111 | |
B | ASN111 | |
C | ASN111 | |
D | ASN111 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17330941 |
Chain | Residue | Details |
A | ASN164 | |
B | ASN164 | |
C | ASN164 | |
D | ASN164 |