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6AJD

Crystal structure of a monometallic dihydropyrimidinase from Pseudomonas aeruginosa PAO1 reveals no lysine carbamylation within the active site

Functional Information from GO Data
ChainGOidnamespacecontents
A0004157molecular_functiondihydropyrimidinase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0046872molecular_functionmetal ion binding
B0004157molecular_functiondihydropyrimidinase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue ZN A 501
ChainResidue
AHIS59
AHIS61
AHIS239
AASP316
AHOH619
AHOH718
AHOH757

site_idAC2
Number of Residues7
Detailsbinding site for residue ZN B 501
ChainResidue
BHIS239
BASP316
BHOH611
BHOH670
BHOH714
BHIS59
BHIS61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9P903
ChainResidueDetails
AHIS59
BHIS61
BTYR155
BHIS183
BHIS239
BSER289
BASP316
BASN337
AHIS61
ATYR155
AHIS183
AHIS239
ASER289
AASP316
AASN337
BHIS59

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000250|UniProtKB:Q9P903
ChainResidueDetails
ALYS150
BLYS150

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000250|UniProtKB:Q9P903
ChainResidueDetails
ALYS150
BLYS150

226707

PDB entries from 2024-10-30

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