3WOR
Crystal structure of the DAP BII octapeptide complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004175 | molecular_function | endopeptidase activity |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
A | 0070009 | molecular_function | serine-type aminopeptidase activity |
B | 0004175 | molecular_function | endopeptidase activity |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0051603 | biological_process | proteolysis involved in protein catabolic process |
B | 0070009 | molecular_function | serine-type aminopeptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 801 |
Chain | Residue |
A | THR598 |
B | GLY594 |
A | PHE600 |
A | ILE639 |
A | HOH919 |
A | HOH1003 |
A | HOH1062 |
A | HOH1140 |
A | HOH1478 |
B | ASP593 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 802 |
Chain | Residue |
A | ASP59 |
A | LYS251 |
A | HIS252 |
A | TRP253 |
A | LYS255 |
A | HOH1248 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 803 |
Chain | Residue |
A | PHE125 |
A | ARG175 |
A | HOH953 |
A | HOH1327 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 804 |
Chain | Residue |
A | TYR89 |
A | LYS208 |
A | ASP212 |
A | ALA322 |
A | ALA326 |
A | ASN329 |
A | GOL806 |
A | HOH1279 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 805 |
Chain | Residue |
A | CYS87 |
A | GLY90 |
A | ALA91 |
A | TYR228 |
A | HOH1029 |
A | HOH1039 |
A | HOH1177 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 806 |
Chain | Residue |
A | ASN101 |
A | GLN318 |
A | GOL804 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 807 |
Chain | Residue |
A | ARG413 |
A | GLU539 |
A | ARG542 |
A | HOH1111 |
A | HOH1465 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 808 |
Chain | Residue |
A | GLU505 |
A | LYS508 |
A | HOH1483 |
B | GLU438 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 809 |
Chain | Residue |
A | LYS47 |
A | GLU635 |
A | HIS665 |
A | HOH1487 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 801 |
Chain | Residue |
A | ASP593 |
A | GLY594 |
A | HOH946 |
B | THR598 |
B | PHE600 |
B | ILE639 |
B | HOH942 |
B | HOH1145 |
B | HOH1150 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 802 |
Chain | Residue |
B | ASP128 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 803 |
Chain | Residue |
A | GLU438 |
B | GLU505 |
B | LYS508 |
B | HOH1234 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 804 |
Chain | Residue |
B | LYS47 |
B | GLU635 |
B | HIS665 |
B | HOH1321 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Beta-decarboxylated aspartate; in form angiotensin-A => ECO:0000269|PubMed:17138938 |
Chain | Residue | Details |
C | ASP1 | |
D | ASP1 | |
A | ALA657 | |
B | ALA86 | |
B | ALA224 | |
B | ALA657 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24827749 |
Chain | Residue | Details |
A | ASN215 | |
A | ASN330 | |
A | GLY655 | |
A | PHE673 | |
B | ASN215 | |
B | ASN330 | |
B | GLY655 | |
B | PHE673 |