5Y52
Crystal Structure of Highly Active BTUO Mutant P287G Improved by Humidity Control at 83% RH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004846 | molecular_function | urate oxidase activity |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0004846 | molecular_function | urate oxidase activity |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| C | 0004846 | molecular_function | urate oxidase activity |
| C | 0006144 | biological_process | purine nucleobase metabolic process |
| D | 0004846 | molecular_function | urate oxidase activity |
| D | 0006144 | biological_process | purine nucleobase metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue AZA A 401 |
| Chain | Residue |
| A | PHE184 |
| B | ALA72 |
| B | THR73 |
| A | LEU195 |
| A | ARG201 |
| A | SER248 |
| A | ILE249 |
| A | GLN250 |
| A | ASN276 |
| A | OXY402 |
| A | HOH673 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue OXY A 402 |
| Chain | Residue |
| A | ASN276 |
| A | GLY302 |
| A | GLN304 |
| A | AZA401 |
| B | THR73 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG298 |
| C | ARG298 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLU119 |
| A | ALA148 |
| A | GLU231 |
| A | ARG234 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue AZA B 401 |
| Chain | Residue |
| A | VAL70 |
| A | ALA72 |
| A | THR73 |
| B | PHE184 |
| B | LEU195 |
| B | ARG201 |
| B | SER248 |
| B | ILE249 |
| B | GLN250 |
| B | ASN276 |
| B | OXY402 |
| B | HOH669 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OXY B 402 |
| Chain | Residue |
| A | THR73 |
| B | ASN276 |
| B | GLY302 |
| B | GLN304 |
| B | AZA401 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | GLU119 |
| B | GLU231 |
| B | ARG234 |
| B | EDO406 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | GLN275 |
| B | TYR301 |
| B | PHE303 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | HIS42 |
| B | ILE43 |
| B | LEU44 |
| B | PHE122 |
| B | PHE140 |
| B | HOH582 |
| B | HOH704 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | GLU123 |
| B | SER143 |
| B | ASN145 |
| B | GLU146 |
| B | EDO403 |
| B | HOH586 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue AZA C 401 |
| Chain | Residue |
| C | PHE184 |
| C | LEU195 |
| C | ARG201 |
| C | SER248 |
| C | ILE249 |
| C | GLN250 |
| C | ASN276 |
| C | OXY402 |
| C | HOH570 |
| D | ALA72 |
| D | THR73 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue OXY C 402 |
| Chain | Residue |
| C | ASN276 |
| C | GLY302 |
| C | GLN304 |
| C | AZA401 |
| D | THR73 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| C | GLU119 |
| C | GLU231 |
| C | ARG234 |
| C | EDO404 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| C | GLU123 |
| C | SER143 |
| C | ASN145 |
| C | GLU146 |
| C | EDO403 |
| C | HOH522 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| C | HIS42 |
| C | ILE43 |
| C | LEU44 |
| C | PHE122 |
| C | PHE140 |
| C | HOH532 |
| C | HOH678 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 406 |
| Chain | Residue |
| C | LYS50 |
| C | HOH615 |
| C | HOH756 |
| D | TYR301 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 401 |
| Chain | Residue |
| D | PHE122 |
| D | PHE140 |
| D | HOH550 |
| D | HOH603 |
| D | HIS42 |
| D | ILE43 |
| D | LEU44 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for residue AZA D 402 |
| Chain | Residue |
| C | ALA72 |
| C | THR73 |
| D | PHE184 |
| D | LEU195 |
| D | ARG201 |
| D | SER248 |
| D | ILE249 |
| D | GLN250 |
| D | ASN276 |
| D | OXY403 |
| D | HOH615 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue OXY D 403 |
| Chain | Residue |
| C | THR73 |
| D | ASN276 |
| D | GLY302 |
| D | GLN304 |
| D | AZA402 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 D 404 |
| Chain | Residue |
| B | ARG298 |
| D | ARG298 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 405 |
| Chain | Residue |
| D | GLU119 |
| D | GLU231 |
| D | ARG234 |
Functional Information from PROSITE/UniProt
| site_id | PS00366 |
| Number of Residues | 28 |
| Details | URICASE Uricase signature. LqLIKVSgNsFvgFirdeYttLpedsnR |
| Chain | Residue | Details |
| A | LEU174-ARG201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Charge relay system; for urate oxidase activity","evidences":[{"source":"UniProtKB","id":"D0VWQ1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of urate oxidase from Bacillus sp.","authoringGroup":["Mycobacterium tuberculosis structural genomics consortium (TB)"]}}]} |
| Chain | Residue | Details |






