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5Y5Q

Crystal structure of the WSSV dUTPase D88N/R158E mutant in complex with dUTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004170molecular_functiondUTP diphosphatase activity
A0006226biological_processdUMP biosynthetic process
A0046081biological_processdUTP catabolic process
B0000287molecular_functionmagnesium ion binding
B0004170molecular_functiondUTP diphosphatase activity
B0006226biological_processdUMP biosynthetic process
B0046081biological_processdUTP catabolic process
C0000287molecular_functionmagnesium ion binding
C0004170molecular_functiondUTP diphosphatase activity
C0006226biological_processdUMP biosynthetic process
C0046081biological_processdUTP catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue DUT A 501
ChainResidue
ATHR84
AHOH616
AHOH632
AHOH634
AHOH639
AHOH676
AHOH690
AHOH710
AHOH712
BARG71
BSER72
AGLY85
BGLY73
BGLN118
BMG201
BHOH306
BHOH368
BHOH369
ATHR86
AILE87
AASN88
ATYR91
ALYS96
AHOH601
AHOH611

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
AHOH604
AHOH618
CDUT202
CHOH385

site_idAC3
Number of Residues5
Detailsbinding site for residue MG B 201
ChainResidue
ADUT501
AHOH601
AHOH712
BHOH306
BHOH369

site_idAC4
Number of Residues25
Detailsbinding site for residue DUT B 202
ChainResidue
BTHR84
BGLY85
BTHR86
BILE87
BASN88
BTYR91
BLYS96
BHOH304
BHOH305
BHOH309
BHOH319
BHOH320
BHOH334
BHOH335
BHOH346
BHOH398
BHOH411
BHOH420
CARG71
CSER72
CGLY73
CGLN118
CMG201
CHOH305
CHOH344

site_idAC5
Number of Residues5
Detailsbinding site for residue MG C 201
ChainResidue
BDUT202
BHOH304
BHOH411
CHOH305
CHOH344

site_idAC6
Number of Residues23
Detailsbinding site for residue DUT C 202
ChainResidue
AARG71
ASER72
AGLY73
AGLN118
AMG502
AHOH604
AHOH618
AHOH641
AHOH681
CTHR84
CGLY85
CTHR86
CILE87
CASN88
CTYR91
CLYS96
CHOH307
CHOH308
CHOH313
CHOH337
CHOH375
CHOH381
CHOH385

220472

PDB entries from 2024-05-29

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