5Y2P
Crystal Structure of Bacillus sp. TB-90 Urate Oxidase Improved by Humidity Control at 89% RH
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue AZA A 401 |
Chain | Residue |
A | PHE184 |
B | TYR11 |
B | ALA72 |
B | THR73 |
A | LEU195 |
A | ARG201 |
A | SER248 |
A | ILE249 |
A | GLN250 |
A | ASN276 |
A | OXY402 |
A | HOH689 |
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 |
B | ARG298 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | HIS42 |
A | ILE43 |
A | LEU44 |
A | PHE122 |
A | PHE140 |
A | HOH622 |
A | HOH625 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | GLU119 |
A | GLU146 |
A | LEU171 |
A | GLU231 |
A | ARG234 |
A | HOH595 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue AZA B 401 |
Chain | Residue |
A | ALA72 |
A | THR73 |
B | PHE184 |
B | ARG201 |
B | SER248 |
B | ILE249 |
B | GLN250 |
B | ASN276 |
B | OXY402 |
B | HOH579 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue OXY B 402 |
Chain | Residue |
A | THR73 |
B | ASN276 |
B | GLY302 |
B | GLN304 |
B | AZA401 |
B | HOH519 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue K B 403 |
Chain | Residue |
B | ILE32 |
B | SER35 |
B | SER38 |
B | ARG133 |
B | HOH605 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | GLU119 |
B | ALA230 |
B | GLU231 |
B | ARG234 |
B | EDO405 |
B | HOH504 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | GLU123 |
B | SER143 |
B | ASN145 |
B | GLU146 |
B | EDO404 |
B | HOH590 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | HIS42 |
B | ILE43 |
B | LEU44 |
B | PHE122 |
B | PHE140 |
B | HOH580 |
B | HOH661 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue EDO B 407 |
Chain | Residue |
B | ARG40 |
B | HIS42 |
B | PHE45 |
B | GLU119 |
B | HOH505 |
B | HOH568 |
B | HOH585 |
B | HOH612 |
B | HOH760 |
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 | 4 |
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 | 2 |
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 | 10 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
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 |