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5UIV

Structure of Thymidylate Kinase from Candida albicans Reveals Origin of Broad Substrate Specificity and a Novel Structural Element.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004550molecular_functionnucleoside diphosphate kinase activity
A0004798molecular_functionthymidylate kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006227biological_processdUDP biosynthetic process
A0006233biological_processdTDP biosynthetic process
A0006235biological_processdTTP biosynthetic process
A0009041molecular_functionUMP/dUMP kinase activity
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046872molecular_functionmetal ion binding
A0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue TMP A 301
ChainResidue
ALYS35
AHOH411
AHOH413
AHOH424
AHOH428
AHOH430
AHOH436
AHOH440
AHOH454
AARG39
ALEU51
APHE67
AARG71
AARG92
AGLY97
ATYR100
ATYR161

site_idAC2
Number of Residues18
Detailsbinding site for residue ADP A 302
ChainResidue
ALEU12
AASP13
AARG14
ASER15
AGLY16
ALYS17
ASER18
ATHR19
AARG153
ALYS154
ALYS194
ATHR195
AILE196
AMG303
AHOH416
AHOH417
AHOH432
AHOH443

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 303
ChainResidue
AASP13
AADP302
AHOH424
AHOH432
AHOH454
AHOH471

site_idAC4
Number of Residues4
Detailsbinding site for residue MG A 304
ChainResidue
AASP13
AGLY155
AGLU162
AHOH450

Functional Information from PROSITE/UniProt
site_idPS01331
Number of Residues13
DetailsTHYMIDYLATE_KINASE Thymidylate kinase signature. ILDRYiySGiAYT
ChainResidueDetails
AILE89-THR101

223790

PDB entries from 2024-08-14

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