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4YL5

Structure of a putative phosphomethylpyrimidine kinase from Acinetobacter baumannii

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0008902molecular_functionhydroxymethylpyrimidine kinase activity
A0008972molecular_functionphosphomethylpyrimidine kinase activity
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016301molecular_functionkinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue EDO A 300
ChainResidue
AGLY86
AMET87
ALEU88
AGLY89
AVAL114
ALEU123
ALEU129
APHE133

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 301
ChainResidue
AMET87
AHOH456
AGLN51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:38306231, ECO:0007744|PDB:4YWR
ChainResidueDetails
AGLY26
AGLN51
AASN118
ASER216

222926

PDB entries from 2024-07-24

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