3WOJ
Crystal structure of the DAP BII
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 | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 801 |
| Chain | Residue |
| A | THR598 |
| A | PHE600 |
| A | ILE639 |
| A | HOH924 |
| A | HOH971 |
| B | ASP593 |
| B | GLY594 |
| B | HOH941 |
| B | HOH1069 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 802 |
| Chain | Residue |
| A | ASP286 |
| A | ASN287 |
| A | GLN290 |
| A | LYS387 |
| A | ARG390 |
| A | HOH1046 |
| B | GLN567 |
| B | GLY568 |
| B | HOH1058 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 803 |
| Chain | Residue |
| A | GLN259 |
| A | PRO260 |
| A | ASP265 |
| A | ARG638 |
| A | HOH1066 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | TRP216 |
| A | TRP218 |
| A | TYR589 |
| A | TRP677 |
| A | GLU678 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 805 |
| Chain | Residue |
| A | LYS153 |
| A | GLU156 |
| A | GLU426 |
| A | LYS543 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 801 |
| Chain | Residue |
| A | ASP593 |
| A | GLY594 |
| A | HOH935 |
| B | THR598 |
| B | PHE600 |
| B | ILE639 |
| B | HOH902 |
| B | HOH994 |
| B | HOH1011 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 802 |
| Chain | Residue |
| B | GLN259 |
| B | PRO260 |
| B | ASP265 |
| B | ARG638 |
| B | HOH966 |
| B | HOH1110 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 803 |
| Chain | Residue |
| A | ASP59 |
| A | LYS251 |
| A | HIS252 |
| A | TRP253 |
| A | LYS255 |
| B | ASP55 |
| B | GLY58 |
| B | ASP59 |
| B | HIS252 |
| B | HOH1018 |
| B | HOH1327 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 804 |
| Chain | Residue |
| B | LYS153 |
| B | GLU156 |
| B | GLU426 |
| B | LYS543 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 805 |
| Chain | Residue |
| A | HIS252 |
| A | HOH1083 |
| B | ASP55 |
| B | HOH1327 |
| B | HOH1330 |
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 | ASN215 | |
| A | ASN330 | |
| A | GLY655 | |
| A | PHE673 | |
| B | ASN215 | |
| B | ASN330 | |
| B | GLY655 | |
| B | PHE673 |
