3WOP
Crystal structure of the DAP BII hexapeptide complex II
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 | 0008233 | molecular_function | peptidase activity |
| A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0008233 | molecular_function | peptidase activity |
| B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| B | 0016787 | molecular_function | hydrolase 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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 801 |
| Chain | Residue |
| A | THR598 |
| A | PHE600 |
| A | HOH919 |
| A | HOH992 |
| A | HOH1037 |
| A | HOH1092 |
| B | ASP593 |
| B | GLY594 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 802 |
| Chain | Residue |
| A | LYS251 |
| A | HIS252 |
| A | TRP253 |
| A | LYS255 |
| A | ASP59 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 803 |
| Chain | Residue |
| A | ASN101 |
| A | GLN318 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | ALA257 |
| A | ASP258 |
| A | GLN259 |
| A | GLY633 |
| A | HOH920 |
| A | HOH1194 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 805 |
| Chain | Residue |
| A | GLU505 |
| A | LYS508 |
| B | GLU438 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 806 |
| Chain | Residue |
| A | LYS47 |
| A | GLU635 |
| A | HIS665 |
| A | HOH1263 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 801 |
| Chain | Residue |
| A | ASP593 |
| A | GLY594 |
| A | HOH1162 |
| B | THR598 |
| B | PHE600 |
| B | ILE639 |
| B | HOH920 |
| B | HOH940 |
| B | HOH1078 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 802 |
| Chain | Residue |
| B | ALA257 |
| B | ASP258 |
| B | GLN259 |
| B | GLY633 |
| B | ARG699 |
| B | ARG702 |
| B | HOH919 |
| B | HOH923 |
| B | HOH953 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 803 |
| Chain | Residue |
| B | LEU127 |
| B | ASP128 |
| B | PHE172 |
| B | LYS251 |
| B | HOH1199 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 804 |
| Chain | Residue |
| B | ASP59 |
| B | LYS251 |
| B | HIS252 |
| B | TRP253 |
| B | LYS255 |
| B | PRO468 |
| B | ALA469 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 805 |
| Chain | Residue |
| B | ARG173 |
| B | ARG175 |
| B | TYR177 |
| B | ASN190 |
| B | HOH952 |
| B | HOH1137 |
| B | HOH1220 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 806 |
| Chain | Residue |
| A | GLU438 |
| B | GLU505 |
| B | LYS508 |
| B | HOH1198 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 807 |
| Chain | Residue |
| B | LYS47 |
| B | GLU635 |
| B | HIS665 |
| B | HOH1167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"24598890","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24827749","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24827749","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
