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4FWL

Crystal structure of Salmonella typhimurium propionate kinase (TdcD) in complex with Phosphate (PO4)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006082biological_processorganic acid metabolic process
A0006083biological_processacetate metabolic process
A0008776molecular_functionacetate kinase activity
A0008980molecular_functionpropionate kinase activity
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
A0046872molecular_functionmetal ion binding
A0070689biological_processL-threonine catabolic process to propionate
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
AHIS175
AMET223
AARG236
AHOH549

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 402
ChainResidue
AHOH585
AHIS175
AHIS203
AGLY205
AASN206
AGLY207

Functional Information from PROSITE/UniProt
site_idPS01075
Number of Residues12
DetailsACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvINcGSSSiK
ChainResidueDetails
AVAL7-LYS18

site_idPS01076
Number of Residues18
DetailsACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. LIvaHlGnGaSIcAvrnG
ChainResidueDetails
ALEU199-GLY216

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01881
ChainResidueDetails
AASP143

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01881
ChainResidueDetails
AASN11
ALYS18
AARG86
AGLY326
AGLU381

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AHIS175
AHIS203
AASP278

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01881
ChainResidueDetails
AHIS175
AARG236

229380

PDB entries from 2024-12-25

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