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5VGM

Crystal structure of dihydroorotase pyrC from Vibrio cholerae in complex with zinc at 1.95 A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004151molecular_functiondihydroorotase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
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
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AKCX98
AHIS135
AHIS173
AZN402
AHOH536

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 402
ChainResidue
AZN401
AHOH536
AHIS13
AHIS15
AKCX98
AASP246

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 403
ChainResidue
AARG17
AASP18
ATHR42
AVAL43

site_idAC4
Number of Residues4
Detailsbinding site for residue ACT A 404
ChainResidue
AARG203
AARG223
BARG203
BARG223

site_idAC5
Number of Residues1
Detailsbinding site for residue ACT A 405
ChainResidue
AARG303

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN B 401
ChainResidue
BKCX98
BHIS135
BHIS173
BZN402
BHOH556

site_idAC7
Number of Residues6
Detailsbinding site for residue ZN B 402
ChainResidue
BHIS13
BHIS15
BKCX98
BASP246
BZN401
BHOH556

site_idAC8
Number of Residues1
Detailsbinding site for residue ACT B 403
ChainResidue
BHOH508

site_idAC9
Number of Residues3
Detailsbinding site for residue CL B 404
ChainResidue
BGLY282
BLYS283
BLEU284

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DWHVHLRdG
ChainResidueDetails
AASP11-GLY19

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. GTDsAPHakgrK
ChainResidueDetails
AGLY244-LYS255

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00219
ChainResidueDetails
AASP246
BASP246

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00219
ChainResidueDetails
AHIS13
BHIS13
BHIS15
BASN41
BHIS135
BHIS173
BLEU218
BASP246
BHIS250
BALA262
AHIS15
AASN41
AHIS135
AHIS173
ALEU218
AASP246
AHIS250
AALA262

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_00219
ChainResidueDetails
AKCX98
BKCX98

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_00219
ChainResidueDetails
AKCX98
BKCX98

223166

PDB entries from 2024-07-31

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