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1XRH

Crystal Structure of Ureidoglycolate Dehydrogenase from Escherichia Coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000256biological_processallantoin catabolic process
A0005737cellular_componentcytoplasm
A0006144biological_processpurine nucleobase metabolic process
A0009040molecular_functionureidoglycolate dehydrogenase activity
A0009442biological_processallantoin assimilation pathway
A0016491molecular_functionoxidoreductase activity
B0000256biological_processallantoin catabolic process
B0005737cellular_componentcytoplasm
B0006144biological_processpurine nucleobase metabolic process
B0009040molecular_functionureidoglycolate dehydrogenase activity
B0009442biological_processallantoin assimilation pathway
B0016491molecular_functionoxidoreductase activity
C0000256biological_processallantoin catabolic process
C0005737cellular_componentcytoplasm
C0006144biological_processpurine nucleobase metabolic process
C0009040molecular_functionureidoglycolate dehydrogenase activity
C0009442biological_processallantoin assimilation pathway
C0016491molecular_functionoxidoreductase activity
D0000256biological_processallantoin catabolic process
D0005737cellular_componentcytoplasm
D0006144biological_processpurine nucleobase metabolic process
D0009040molecular_functionureidoglycolate dehydrogenase activity
D0009442biological_processallantoin assimilation pathway
D0016491molecular_functionoxidoreductase activity
E0000256biological_processallantoin catabolic process
E0005737cellular_componentcytoplasm
E0006144biological_processpurine nucleobase metabolic process
E0009040molecular_functionureidoglycolate dehydrogenase activity
E0009442biological_processallantoin assimilation pathway
E0016491molecular_functionoxidoreductase activity
F0000256biological_processallantoin catabolic process
F0005737cellular_componentcytoplasm
F0006144biological_processpurine nucleobase metabolic process
F0009040molecular_functionureidoglycolate dehydrogenase activity
F0009442biological_processallantoin assimilation pathway
F0016491molecular_functionoxidoreductase activity
G0000256biological_processallantoin catabolic process
G0005737cellular_componentcytoplasm
G0006144biological_processpurine nucleobase metabolic process
G0009040molecular_functionureidoglycolate dehydrogenase activity
G0009442biological_processallantoin assimilation pathway
G0016491molecular_functionoxidoreductase activity
H0000256biological_processallantoin catabolic process
H0005737cellular_componentcytoplasm
H0006144biological_processpurine nucleobase metabolic process
H0009040molecular_functionureidoglycolate dehydrogenase activity
H0009442biological_processallantoin assimilation pathway
H0016491molecular_functionoxidoreductase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23284870
ChainResidueDetails
AHIS118
BHIS118
CHIS118
DHIS118
EHIS118
FHIS118
GHIS118
HHIS118

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000305|PubMed:23284870, ECO:0007744|PDB:4H8A
ChainResidueDetails
ASER142
CASP176
CLYS226
CGLY308
DSER142
DASP176
DLYS226
DGLY308
ESER142
EASP176
ELYS226
AASP176
EGLY308
FSER142
FASP176
FLYS226
FGLY308
GSER142
GASP176
GLYS226
GGLY308
HSER142
ALYS226
HASP176
HLYS226
HGLY308
AGLY308
BSER142
BASP176
BLYS226
BGLY308
CSER142

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Plays a crucial role in stabilizing the binding of (S)-ureidoglycolate => ECO:0000305|PubMed:23284870
ChainResidueDetails
AARG50
BARG50
CARG50
DARG50
EARG50
FARG50
GARG50
HARG50

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
AHIS46

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
BHIS46

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
CHIS46

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
DHIS46

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
EHIS46

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
FHIS46

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
GHIS46

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1s20
ChainResidueDetails
HHIS46

226707

PDB entries from 2024-10-30

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