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5Y2P

Crystal Structure of Bacillus sp. TB-90 Urate Oxidase Improved by Humidity Control at 89% 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
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue AZA A 401
ChainResidue
APHE184
BTYR11
BALA72
BTHR73
ALEU195
AARG201
ASER248
AILE249
AGLN250
AASN276
AOXY402
AHOH689

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
BARG298

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 404
ChainResidue
AHIS42
AILE43
ALEU44
APHE122
APHE140
AHOH622
AHOH625

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 405
ChainResidue
AGLU119
AGLU146
ALEU171
AGLU231
AARG234
AHOH595

site_idAC6
Number of Residues10
Detailsbinding site for residue AZA B 401
ChainResidue
AALA72
ATHR73
BPHE184
BARG201
BSER248
BILE249
BGLN250
BASN276
BOXY402
BHOH579

site_idAC7
Number of Residues6
Detailsbinding site for residue OXY B 402
ChainResidue
ATHR73
BASN276
BGLY302
BGLN304
BAZA401
BHOH519

site_idAC8
Number of Residues5
Detailsbinding site for residue K B 403
ChainResidue
BILE32
BSER35
BSER38
BARG133
BHOH605

site_idAC9
Number of Residues6
Detailsbinding site for residue EDO B 404
ChainResidue
BGLU119
BALA230
BGLU231
BARG234
BEDO405
BHOH504

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO B 405
ChainResidue
BGLU123
BSER143
BASN145
BGLU146
BEDO404
BHOH590

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO B 406
ChainResidue
BHIS42
BILE43
BLEU44
BPHE122
BPHE140
BHOH580
BHOH661

site_idAD3
Number of Residues9
Detailsbinding site for residue EDO B 407
ChainResidue
BARG40
BHIS42
BPHE45
BGLU119
BHOH505
BHOH568
BHOH585
BHOH612
BHOH760

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 Residues4
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 Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q00511","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
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

239149

PDB entries from 2025-07-23

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