5CMX
X-ray structure of the complex between human alpha thrombin and a duplex/quadruplex 31-mer DNA aptamer
Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0004252 | molecular_function | serine-type endopeptidase activity |
H | 0005509 | molecular_function | calcium ion binding |
H | 0006508 | biological_process | proteolysis |
H | 0007596 | biological_process | blood coagulation |
L | 0004252 | molecular_function | serine-type endopeptidase activity |
L | 0005576 | cellular_component | extracellular region |
L | 0006508 | biological_process | proteolysis |
L | 0007596 | biological_process | blood coagulation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue 0G6 H 401 |
Chain | Residue |
H | HIS57 |
H | TRP215 |
H | GLY216 |
H | GLY219 |
H | HOH515 |
H | TYR60 |
H | LEU99 |
H | ASP189 |
H | ALA190 |
H | GLU192 |
H | GLY193 |
H | SER195 |
H | SER214 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue K A 101 |
Chain | Residue |
A | DG9 |
A | DG10 |
A | DG13 |
A | DG14 |
A | DG18 |
A | DG19 |
A | DG22 |
A | DG23 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"description":"Charge relay system"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |