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4NQ3

Crystal structure of cyanuic acid hydrolase from A. caulinodans

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 BR8 A 401
ChainResidue
AGLY45
AGLY334
AARG52
ASER79
AGLY80
AARG188
ASER226
ASER227
AARG314
ASER333

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG95
AARG111
AHOH534

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AARG129
AHOH543
AHOH569

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AALA112
AHIS113
AARG137
AHOH531

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AASP179
ATHR180
ALEU181
AHOH536
BASP304
BPRO309

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
AALA12
ATHR161
AARG164
AHOH520

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 407
ChainResidue
APRO2
AALA141
AALA142
ATRP245

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BR8 A 408
ChainResidue
AALA176
ATHR177
ASER178
BLYS182
BSO4402
BHOH515

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 409
ChainResidue
AGLU287
AGLY336
AGLN339
AGLY340
APRO341
AGLY344

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 410
ChainResidue
AGLU329
AHOH530
AHOH604

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BR8 B 401
ChainResidue
BGLY45
BARG52
BSER79
BGLY80
BARG188
BSER226
BSER227
BARG314
BSER333
BGLY334

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
ABR8408
BTHR177
BSER178
BASP179

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
ALYS297
BARG8
BGLU278
BGLU329

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 404
ChainResidue
BARG129
BHOH534

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 405
ChainResidue
BARG295
BGLY296
BHOH518
BHOH526

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 406
ChainResidue
BGLU287
BGLY336
BGLN339
BGLY340
BPRO341
BGLY344

Functional Information from PROSITE/UniProt
site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LGHEIVVLGMS
ChainResidueDetails
ALEU232-SER242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24915109
ChainResidueDetails
ALYS156
BLYS156

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24915109
ChainResidueDetails
ASER226
BSER226

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:24915109
ChainResidueDetails
AARG52
AGLY340
APRO341
AGLY344
BARG52
BSER79
BARG188
BSER226
BGLU287
BARG314
BSER333
ASER79
BGLY336
BGLN339
BGLY340
BPRO341
BGLY344
AARG188
ASER226
AGLU287
AARG314
ASER333
AGLY336
AGLN339

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_01989
ChainResidueDetails
ATHR310
BTHR310

222036

PDB entries from 2024-07-03

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