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5Y52

Crystal Structure of Highly Active BTUO Mutant P287G Improved by Humidity Control at 83% RH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004846molecular_functionurate oxidase activity
A0006144biological_processpurine nucleobase metabolic process
B0004846molecular_functionurate oxidase activity
B0006144biological_processpurine nucleobase metabolic process
C0004846molecular_functionurate oxidase activity
C0006144biological_processpurine nucleobase metabolic process
D0004846molecular_functionurate oxidase activity
D0006144biological_processpurine nucleobase metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue AZA A 401
ChainResidue
APHE184
BALA72
BTHR73
ALEU195
AARG201
ASER248
AILE249
AGLN250
AASN276
AOXY402
AHOH673

site_idAC2
Number of Residues5
Detailsbinding site for residue OXY A 402
ChainResidue
AASN276
AGLY302
AGLN304
AAZA401
BTHR73

site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 A 403
ChainResidue
AARG298
CARG298

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU119
AALA148
AGLU231
AARG234

site_idAC5
Number of Residues12
Detailsbinding site for residue AZA B 401
ChainResidue
AVAL70
AALA72
ATHR73
BPHE184
BLEU195
BARG201
BSER248
BILE249
BGLN250
BASN276
BOXY402
BHOH669

site_idAC6
Number of Residues5
Detailsbinding site for residue OXY B 402
ChainResidue
ATHR73
BASN276
BGLY302
BGLN304
BAZA401

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO B 403
ChainResidue
BGLU119
BGLU231
BARG234
BEDO406

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO B 404
ChainResidue
BGLN275
BTYR301
BPHE303

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO B 405
ChainResidue
BHIS42
BILE43
BLEU44
BPHE122
BPHE140
BHOH582
BHOH704

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO B 406
ChainResidue
BGLU123
BSER143
BASN145
BGLU146
BEDO403
BHOH586

site_idAD2
Number of Residues11
Detailsbinding site for residue AZA C 401
ChainResidue
CPHE184
CLEU195
CARG201
CSER248
CILE249
CGLN250
CASN276
COXY402
CHOH570
DALA72
DTHR73

site_idAD3
Number of Residues5
Detailsbinding site for residue OXY C 402
ChainResidue
CASN276
CGLY302
CGLN304
CAZA401
DTHR73

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO C 403
ChainResidue
CGLU119
CGLU231
CARG234
CEDO404

site_idAD5
Number of Residues6
Detailsbinding site for residue EDO C 404
ChainResidue
CGLU123
CSER143
CASN145
CGLU146
CEDO403
CHOH522

site_idAD6
Number of Residues7
Detailsbinding site for residue EDO C 405
ChainResidue
CHIS42
CILE43
CLEU44
CPHE122
CPHE140
CHOH532
CHOH678

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO C 406
ChainResidue
CLYS50
CHOH615
CHOH756
DTYR301

site_idAD8
Number of Residues7
Detailsbinding site for residue EDO D 401
ChainResidue
DPHE122
DPHE140
DHOH550
DHOH603
DHIS42
DILE43
DLEU44

site_idAD9
Number of Residues11
Detailsbinding site for residue AZA D 402
ChainResidue
CALA72
CTHR73
DPHE184
DLEU195
DARG201
DSER248
DILE249
DGLN250
DASN276
DOXY403
DHOH615

site_idAE1
Number of Residues5
Detailsbinding site for residue OXY D 403
ChainResidue
CTHR73
DASN276
DGLY302
DGLN304
DAZA402

site_idAE2
Number of Residues2
Detailsbinding site for residue SO4 D 404
ChainResidue
BARG298
DARG298

site_idAE3
Number of Residues3
Detailsbinding site for residue EDO D 405
ChainResidue
DGLU119
DGLU231
DARG234

Functional Information from PROSITE/UniProt
site_idPS00366
Number of Residues28
DetailsURICASE Uricase signature. LqLIKVSgNsFvgFirdeYttLpedsnR
ChainResidueDetails
ALEU174-ARG201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Charge relay system; for urate oxidase activity","evidences":[{"source":"UniProtKB","id":"D0VWQ1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding 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)"]}}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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