Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3SLC

Crystal structure of apo form of acetate kinase (AckA) from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006082biological_processorganic acid metabolic process
A0006083biological_processacetate metabolic process
A0006085biological_processacetyl-CoA biosynthetic 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
A0047900molecular_functionformate kinase activity
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006082biological_processorganic acid metabolic process
B0006083biological_processacetate metabolic process
B0006085biological_processacetyl-CoA biosynthetic process
B0008776molecular_functionacetate kinase activity
B0008980molecular_functionpropionate kinase activity
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
B0046872molecular_functionmetal ion binding
B0047900molecular_functionformate kinase activity
C0000287molecular_functionmagnesium ion binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006082biological_processorganic acid metabolic process
C0006083biological_processacetate metabolic process
C0006085biological_processacetyl-CoA biosynthetic process
C0008776molecular_functionacetate kinase activity
C0008980molecular_functionpropionate kinase activity
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
C0046872molecular_functionmetal ion binding
C0047900molecular_functionformate kinase activity
D0000287molecular_functionmagnesium ion binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006082biological_processorganic acid metabolic process
D0006083biological_processacetate metabolic process
D0006085biological_processacetyl-CoA biosynthetic process
D0008776molecular_functionacetate kinase activity
D0008980molecular_functionpropionate kinase activity
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
D0046872molecular_functionmetal ion binding
D0047900molecular_functionformate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AASN267
AHOH453
BPHE253

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 501
ChainResidue
BGLU388
BHOH458

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
BTHR242
BARG243
BGLY212
BGLY214
BMET240
BGLY241

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO D 503
ChainResidue
DLYS142
DASP143

Functional Information from PROSITE/UniProt
site_idPS01075
Number of Residues12
DetailsACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvLNcGSSSlK
ChainResidueDetails
AVAL6-LYS17

site_idPS01076
Number of Residues18
DetailsACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. IItcHlGnGgSVsAirnG
ChainResidueDetails
AILE206-GLY223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AASP150
BASP150
CASP150
DASP150

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AASP285
AGLY333
AGLU387
BASN10
BLYS17
BARG91
BHIS210
BASP285
BGLY333
BGLU387
CASN10
CLYS17
CARG91
CHIS210
CASP285
CGLY333
CGLU387
DASN10
DLYS17
DARG91
DHIS210
DASP285
DGLY333
DGLU387
AASN10
ALYS17
AARG91
AHIS210

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
CARG243
DHIS182
DARG243
AHIS182
AARG243
BHIS182
BARG243
CHIS182

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon