3WON
Crystal structure of the DAP BII dipeptide complex III
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 803 |
Chain | Residue |
A | THR598 |
B | HOH967 |
A | PHE600 |
A | ILE639 |
A | HOH919 |
A | HOH1123 |
A | HOH1387 |
A | HOH1481 |
B | ASP593 |
B | GLY594 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 804 |
Chain | Residue |
A | ASP59 |
A | LYS251 |
A | HIS252 |
A | TRP253 |
A | LYS255 |
A | HOH1215 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 805 |
Chain | Residue |
A | GLY68 |
A | ARG175 |
A | HOH950 |
A | HOH1272 |
A | HOH1338 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 806 |
Chain | Residue |
A | ARG413 |
A | LEU535 |
A | GLU539 |
A | ARG542 |
A | HOH1098 |
A | HOH1373 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 807 |
Chain | Residue |
A | ALA257 |
A | ASP258 |
A | ARG699 |
A | HOH920 |
A | HOH1298 |
A | HOH1421 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN A 808 |
Chain | Residue |
A | GLU635 |
A | HIS665 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 809 |
Chain | Residue |
A | GLU505 |
A | LYS508 |
A | HOH1409 |
B | GLU438 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 803 |
Chain | Residue |
A | ASP593 |
A | GLY594 |
B | THR598 |
B | PHE600 |
B | ILE639 |
B | HOH921 |
B | HOH943 |
B | HOH1120 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 804 |
Chain | Residue |
B | ALA257 |
B | ASP258 |
B | ARG699 |
B | HOH920 |
B | HOH924 |
B | HOH958 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 805 |
Chain | Residue |
B | ASP59 |
B | LYS251 |
B | HIS252 |
B | TRP253 |
B | LYS255 |
B | PRO468 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 806 |
Chain | Residue |
B | GLY68 |
B | ARG175 |
B | ASN190 |
B | HOH957 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 807 |
Chain | Residue |
B | LYS47 |
B | GLU635 |
B | HIS665 |
B | HOH1264 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 808 |
Chain | Residue |
A | GLU438 |
B | GLU505 |
B | LYS508 |
site_id | BC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR LINKED RESIDUES A 801 to 802 |
Chain | Residue |
A | HIS86 |
A | ASN215 |
A | TRP216 |
A | ARG220 |
A | ASN330 |
A | ILE652 |
A | THR653 |
A | GLY654 |
A | GLY655 |
A | SER657 |
A | PHE673 |
A | ASP674 |
A | GLY675 |
A | SER679 |
A | HOH940 |
A | HOH1223 |
A | HOH1413 |
site_id | BC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR LINKED RESIDUES B 801 to 802 |
Chain | Residue |
B | GLY675 |
B | SER679 |
B | HOH953 |
B | HOH980 |
B | HOH1265 |
B | HIS86 |
B | ASN215 |
B | TRP216 |
B | ARG220 |
B | ASN330 |
B | ILE652 |
B | THR653 |
B | GLY654 |
B | GLY655 |
B | SER657 |
B | PHE673 |
B | ASP674 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:24598890, ECO:0000305|PubMed:24827749 |
Chain | Residue | Details |
A | HIS86 | |
A | ASP224 | |
A | SER657 | |
B | HIS86 | |
B | ASP224 | |
B | SER657 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24827749 |
Chain | Residue | Details |
A | GLY655 | |
A | PHE673 | |
B | ASN215 | |
B | ASN330 | |
B | GLY655 | |
B | PHE673 | |
A | ASN215 | |
A | ASN330 |