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3GRI

The Crystal Structure of a Dihydroorotase from Staphylococcus aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004038molecular_functionallantoinase activity
A0004151molecular_functiondihydroorotase activity
A0005737cellular_componentcytoplasm
A0006145biological_processpurine nucleobase catabolic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0008270molecular_functionzinc ion binding
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
A0044205biological_process'de novo' UMP biosynthetic process
A0046872molecular_functionmetal ion binding
B0004038molecular_functionallantoinase activity
B0004151molecular_functiondihydroorotase activity
B0005737cellular_componentcytoplasm
B0006145biological_processpurine nucleobase catabolic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0008270molecular_functionzinc ion binding
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
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 500
ChainResidue
AHIS58
AHIS60
AASP303
AHOH491
AHOH658

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 600
ChainResidue
AILE124
ATHR125
AHOH482

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
ATHR86
ATYR364
AASP374
AHOH458
ATHR85

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 700
ChainResidue
APHE391
ASER393
AHOH490
AHOH527
AHOH610
AHOH628

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 701
ChainResidue
AGLU104
AGLU142
AGLY199
AHOH433
AHOH517

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 500
ChainResidue
BHIS58
BHIS60
BASP303
BHOH492

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 600
ChainResidue
BILE124
BTHR125
BHOH551

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 700
ChainResidue
BPHE391
BSER393
BHOH540
BHOH665

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 701
ChainResidue
BGLU104
BGLU142
BGLY199
BHOH479
BHOH493

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DVHVHLReP
ChainResidueDetails
AASP56-PRO64

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHardeK
ChainResidueDetails
AALA301-LYS312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00220
ChainResidueDetails
AASP303
BASP303

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220
ChainResidueDetails
AHIS58
APHE321
BHIS58
BHIS60
BASN92
BASP150
BHIS177
BHIS230
BASN276
BASP303
BHIS307
AHIS60
BPHE321
AASN92
AASP150
AHIS177
AHIS230
AASN276
AASP303
AHIS307

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PDB entries from 2024-04-24

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