5CBP
Crystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree C
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue FLC A 201 |
| Chain | Residue |
| A | GLY10 |
| A | GOL206 |
| A | HOH304 |
| A | HOH329 |
| B | TYR273 |
| A | THR11 |
| A | ASP51 |
| A | SER52 |
| A | THR53 |
| A | GLY82 |
| A | THR83 |
| A | ASP84 |
| A | SER109 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 202 |
| Chain | Residue |
| A | PHE44 |
| A | ASN70 |
| A | LYS73 |
| A | TYR74 |
| B | ARG240 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 203 |
| Chain | Residue |
| A | VAL71 |
| A | LYS72 |
| A | TYR74 |
| A | ASP75 |
| A | PRO101 |
| A | ILE102 |
| B | ASN319 |
| B | ARG325 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue IPA A 204 |
| Chain | Residue |
| A | MET1 |
| A | ASP38 |
| A | CYS39 |
| A | GLU40 |
| A | ASP41 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue IPA A 205 |
| Chain | Residue |
| A | SER159 |
| A | ARG160 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 206 |
| Chain | Residue |
| A | ASP84 |
| A | LYS154 |
| A | THR157 |
| A | FLC201 |
| A | HOH309 |
| B | GLY233 |
| B | ALA234 |
| B | ARG272 |
| B | TYR273 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 207 |
| Chain | Residue |
| A | THR132 |
| A | SER133 |
| A | GLY134 |
| A | ILE170 |
| A | ILE171 |
| A | VAL180 |
| A | VAL181 |
| A | ASN182 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue IPA A 208 |
| Chain | Residue |
| A | LEU45 |
| A | ASP46 |
| A | LYS48 |
| A | VAL50 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 209 |
| Chain | Residue |
| A | GLU22 |
| A | ALA23 |
| A | SER26 |
| A | GLU29 |
| A | ASN49 |
| A | ASP51 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | VAL268 |
| B | ASP269 |
| B | LEU270 |
| B | THR271 |
| B | PRO286 |
| B | GLY288 |
| B | ARG317 |
Functional Information from PROSITE/UniProt
| site_id | PS00917 |
| Number of Residues | 11 |
| Details | ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GiIvtHGTDTL |
| Chain | Residue | Details |
| A | GLY76-LEU86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Region: {"description":"Important for activity at high temperatures","evidences":[{"source":"PubMed","id":"33303914","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; O-isoaspartyl threonine intermediate","evidences":[{"source":"PubMed","id":"25478837","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"25478837","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25478837","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NJE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5B5U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
