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2Z00

Crystal structure of dihydroorotase from Thermus thermophilus

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1004
ChainResidue
AHIS55
AHIS57
AASP147
AASP306
AZN1006

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1006
ChainResidue
AASP147
AHIS174
AHIS233
AZN1004

Functional Information from PROSITE/UniProt
site_idPS00482
Number of Residues9
DetailsDIHYDROOROTASE_1 Dihydroorotase signature 1. DLHAHLReP
ChainResidueDetails
AASP53-PRO61

site_idPS00483
Number of Residues12
DetailsDIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHtlaeK
ChainResidueDetails
AALA304-LYS315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00220
ChainResidueDetails
AASP306

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000269|Ref.2, ECO:0007744|PDB:2Z00
ChainResidueDetails
AHIS55
AHIS57
AASP147
AHIS174
AHIS233
AASP306

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220
ChainResidueDetails
AHIS310
APHE324
AASN89

219869

PDB entries from 2024-05-15

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