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3E74

Crystal structure of E. coli allantoinase with iron ions at the metal center

Functional Information from GO Data
ChainGOidnamespacecontents
A0000256biological_processallantoin catabolic process
A0004038molecular_functionallantoinase activity
A0005737cellular_componentcytoplasm
A0006144biological_processpurine nucleobase metabolic process
A0006145biological_processpurine nucleobase catabolic process
A0008270molecular_functionzinc ion binding
A0009442biological_processallantoin assimilation pathway
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
A0050897molecular_functioncobalt ion binding
B0000256biological_processallantoin catabolic process
B0004038molecular_functionallantoinase activity
B0005737cellular_componentcytoplasm
B0006144biological_processpurine nucleobase metabolic process
B0006145biological_processpurine nucleobase catabolic process
B0008270molecular_functionzinc ion binding
B0009442biological_processallantoin assimilation pathway
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
B0050897molecular_functioncobalt ion binding
C0000256biological_processallantoin catabolic process
C0004038molecular_functionallantoinase activity
C0005737cellular_componentcytoplasm
C0006144biological_processpurine nucleobase metabolic process
C0006145biological_processpurine nucleobase catabolic process
C0008270molecular_functionzinc ion binding
C0009442biological_processallantoin assimilation pathway
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0046872molecular_functionmetal ion binding
C0050897molecular_functioncobalt ion binding
D0000256biological_processallantoin catabolic process
D0004038molecular_functionallantoinase activity
D0005737cellular_componentcytoplasm
D0006144biological_processpurine nucleobase metabolic process
D0006145biological_processpurine nucleobase catabolic process
D0008270molecular_functionzinc ion binding
D0009442biological_processallantoin assimilation pathway
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0046872molecular_functionmetal ion binding
D0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 454
ChainResidue
AHIS59
AHIS61
AKCX146
AASP315
AFE455

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 455
ChainResidue
AHOH456
AKCX146
AHIS186
AHIS242
AFE454

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 454
ChainResidue
BKCX146
BHIS186
BHIS242
BFE455
BHOH684

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 455
ChainResidue
BHIS59
BHIS61
BKCX146
BASP315
BFE454

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE C 454
ChainResidue
CKCX146
CHIS186
CHIS242
CFE455
CHOH531
CHOH722

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE C 455
ChainResidue
CHIS59
CHIS61
CKCX146
CASP315
CFE454

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE D 454
ChainResidue
DKCX146
DHIS186
DHIS242
DFE455

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE D 455
ChainResidue
DHIS59
DHIS61
DKCX146
DASP315
DFE454

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"via carbamate group","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j79
ChainResidueDetails
AASP315

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j79
ChainResidueDetails
BASP315

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j79
ChainResidueDetails
CASP315

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j79
ChainResidueDetails
DASP315

239492

PDB entries from 2025-07-30

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