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4BVQ

Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.

Replaces:  3ZGR
Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0018753molecular_functioncyanuric acid amidohydrolase activity
A0019381biological_processatrazine catabolic process
A0046872molecular_functionmetal ion binding
B0016787molecular_functionhydrolase activity
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0018753molecular_functioncyanuric acid amidohydrolase activity
B0019381biological_processatrazine catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 1364
ChainResidue
BGLY45
BHOH2088
BSER83
BGLY84
BSER232
BARG324
BSER343
BGLY344
BHOH2032
BHOH2033

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 1364
ChainResidue
ASER83
AGLY84
ASER232
AARG324
ASER343
AGLY344
AHOH2029
AHOH2030
AHOH2068

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1365
ChainResidue
BGLU297
BALA346
BGLN349
BPRO351
BGLY354
BHOH2150

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1365
ChainResidue
AGLU297
AALA346
AGLN349
APRO351
AGLY354

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 1366
ChainResidue
AARG305
BASP283
BVAL334
BGLY336

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 1367
ChainResidue
BARG8
BMET286
BILE289
BHIS337

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 1366
ChainResidue
AASP283
ASER333
AVAL334
AVAL335
AGLY336
AHOH2131
BARG305

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PEG A 1367
ChainResidue
ALYS142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01989
ChainResidueDetails
ALYS162
BLYS162

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01989
ChainResidueDetails
ASER232
BSER232

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:23651355
ChainResidueDetails
AARG52
AGLY350
APRO351
AGLY354
BARG52
BSER83
BARG194
BSER232
BGLU297
BARG324
BSER343
ASER83
BALA346
BGLN349
BGLY350
BPRO351
BGLY354
AARG194
ASER232
AGLU297
AARG324
ASER343
AALA346
AGLN349

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000305|PubMed:23651355
ChainResidueDetails
ATHR320
BTHR320

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PDB entries from 2024-11-06

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