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3MWA

Crystal structure of Plasmodium falciparum orotidine 5'-monophosphate decarboxylase covalently modified by 2-prime-fluoro-6-iodo-UMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
A0005515molecular_functionprotein binding
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0044205biological_process'de novo' UMP biosynthetic process
B0004590molecular_functionorotidine-5'-phosphate decarboxylase activity
B0005515molecular_functionprotein binding
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0044205biological_process'de novo' UMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE UFT A 1000
ChainResidue
AASP23
AASN291
AGLY293
AARG294
AHOH337
AHOH347
AHOH361
AHOH374
AHOH399
BASP141
BILE142
ALYS102
BTHR145
AASN104
AASP136
ALYS138
ATHR194
ATHR195
APRO264
AGLN269

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE UFT B 1000
ChainResidue
AASP141
AILE142
ATHR145
BASP23
BLYS102
BASN104
BASP136
BLYS138
BTHR194
BTHR195
BPRO264
BGLN269
BASN291
BGLY293
BARG294
BHOH329
BHOH335
BHOH343
BHOH348
BHOH356

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 2000
ChainResidue
AASN299
APRO300
AMET308
AGLN312

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 3000
ChainResidue
BLYS147
BARG150
BASP179
BGLU180
BGLU181
BHOH475

Functional Information from PROSITE/UniProt
site_idPS00156
Number of Residues14
DetailsOMPDECASE Orotidine 5'-phosphate decarboxylase active site. TIlDmKinDIGnTV
ChainResidueDetails
ATHR133-VAL146

219869

PDB entries from 2024-05-15

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