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4CQB

The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
A0018764molecular_functionN-isopropylammelide isopropylaminohydrolase activity
A0019381biological_processatrazine catabolic process
A0046872molecular_functionmetal ion binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016814molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
B0018764molecular_functionN-isopropylammelide isopropylaminohydrolase activity
B0019381biological_processatrazine catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 1404
ChainResidue
AHIS60
AHIS62
AHIS217
AASP303
AMLI1407
AHOH2028

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 1404
ChainResidue
BASP303
BMLI1408
BHOH2037
BHIS60
BHIS62
BHIS217

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 1405
ChainResidue
AMET286
AVAL288
AILE289
AHOH2188
AHOH2210

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1405
ChainResidue
BLYS42
BILE394
BHOH2247

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS B 1406
ChainResidue
AHOH2215
BTYR82
BTRP251
BASP303
BASN304
BTRP309
BVAL310
BMLI1408

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 1406
ChainResidue
ATYR82
AHIS219
ATRP251
AASP303
AVAL310
AMLI1407
AHOH2181

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS B 1407
ChainResidue
BTYR227
BASN230
BGLU263

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MLI B 1408
ChainResidue
BHIS62
BLYS65
BPHE158
BGLN160
BHIS217
BHIS219
BASN304
BTRP309
BZN1404
BDMS1406
BHOH2037

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLI A 1407
ChainResidue
AHIS62
ALYS65
AGLN160
AHIS217
AHIS219
AASN304
ATRP309
AZN1404
ADMS1406
AHOH2028

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MLI A 1408
ChainResidue
ATYR227
AASN230
AGLU263
AHOH2176

Functional Information from PROSITE/UniProt
site_idPS01137
Number of Residues9
DetailsTATD_1 TatD deoxyribonuclease family signature 1. FVDAHtHMD
ChainResidueDetails
APHE56-ASP64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:26390431
ChainResidueDetails
AHIS249
BHIS249

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3
ChainResidueDetails
AHIS60
AHIS62
AHIS217
AASP303
BHIS60
BHIS62
BHIS217
BASP303

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PDB entries from 2024-07-10

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