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4CQC

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1404
ChainResidue
AHIS60
AHIS62
AHIS217
AHIS249
AASP303

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 1404
ChainResidue
BASP303
BHIS60
BHIS62
BHIS217
BHIS249

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1405
ChainResidue
BVAL196
BVAL196
BGLU197
BGLU197

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1405
ChainResidue
AVAL196
AVAL196
AGLU197
AGLU197

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EPE A 1406
ChainResidue
ATHR191
AASN194
ATYR227
AASN230
ATRP260
AGLU263

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EPE B 1406
ChainResidue
BTHR191
BASN194
BTYR227
BASN230
BTRP260

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

223166

PDB entries from 2024-07-31

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