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6L0B

Crystal structure of dihydroorotase in complex with fluorouracil from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A0019856biological_processpyrimidine nucleobase biosynthetic process
A0044205biological_process'de novo' UMP biosynthetic process
A0046872molecular_functionmetal ion binding
B0004151molecular_functiondihydroorotase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
B0019856biological_processpyrimidine nucleobase biosynthetic process
B0044205biological_process'de novo' UMP biosynthetic process
B0046872molecular_functionmetal ion binding
C0004151molecular_functiondihydroorotase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
C0006221biological_processpyrimidine nucleotide biosynthetic process
C0008270molecular_functionzinc ion binding
C0016787molecular_functionhydrolase activity
C0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
C0019856biological_processpyrimidine nucleobase biosynthetic process
C0044205biological_process'de novo' UMP biosynthetic process
C0046872molecular_functionmetal ion binding
D0004151molecular_functiondihydroorotase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0008270molecular_functionzinc ion binding
D0016787molecular_functionhydrolase activity
D0016812molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
D0019856biological_processpyrimidine nucleobase biosynthetic process
D0044205biological_process'de novo' UMP biosynthetic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS14
AHIS16
AKCX98
AASP258
AZN402
AURF403

site_idAC2
Number of Residues5
Detailsbinding site for residue ZN A 402
ChainResidue
AZN401
AURF403
AKCX98
AHIS137
AHIS180

site_idAC3
Number of Residues11
Detailsbinding site for residue URF A 403
ChainResidue
AHIS16
AARG18
AASN43
ATHR105
ATHR106
AASP258
AALA260
AHIS262
AALA275
AZN401
AZN402

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN C 401
ChainResidue
CKCX98
CHIS137
CHIS180
CZN402
CURF403

site_idAC5
Number of Residues6
Detailsbinding site for residue ZN C 402
ChainResidue
CHIS14
CHIS16
CKCX98
CASP258
CZN401
CURF403

site_idAC6
Number of Residues13
Detailsbinding site for residue URF C 403
ChainResidue
CHIS16
CARG18
CASN43
CKCX98
CTHR105
CTHR106
CASP258
CALA260
CHIS262
CALA275
CZN401
CZN402
CHOH503

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS14
BHIS16
BKCX98
BASP258
BZN402
BURF403

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN B 402
ChainResidue
BKCX98
BHIS137
BHIS180
BZN401
BURF403

site_idAC9
Number of Residues15
Detailsbinding site for residue URF B 403
ChainResidue
BHIS16
BARG18
BASN43
BKCX98
BTHR105
BTHR106
BHIS137
BHIS180
BLYS230
BASP258
BHIS262
BALA275
BZN401
BZN402
BHOH535

site_idAD1
Number of Residues5
Detailsbinding site for residue ZN D 401
ChainResidue
DKCX98
DHIS137
DHIS180
DZN402
DURF403

site_idAD2
Number of Residues6
Detailsbinding site for residue ZN D 402
ChainResidue
DHIS14
DHIS16
DKCX98
DASP258
DZN401
DURF403

site_idAD3
Number of Residues14
Detailsbinding site for residue URF D 403
ChainResidue
DHIS16
DARG18
DASN43
DKCX98
DTHR105
DTHR106
DLYS230
DASP258
DALA260
DHIS262
DALA275
DGLY276
DZN401
DZN402

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DMHVHVReG
ChainResidueDetails
AASP12-GLY20

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. GSDsAPHpvqnK
ChainResidueDetails
AGLY256-LYS267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05020
ChainResidueDetails
CHIS180
CASP258
BHIS14
BHIS16
BHIS137
BHIS180
BASP258
DHIS14
DHIS16
DHIS137
DHIS180
DASP258
AHIS137
AHIS180
AASP258
CHIS14
CHIS16
CHIS137
AHIS14
AHIS16

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: via carbamate group => ECO:0000250|UniProtKB:P05020
ChainResidueDetails
CKCX98
BKCX98
DKCX98
AKCX98

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-carboxylysine => ECO:0000250|UniProtKB:P05020
ChainResidueDetails
AKCX98
CKCX98
BKCX98
DKCX98

221051

PDB entries from 2024-06-12

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