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3SK3

Crystal structure of Salmonella typhimurium acetate kinase (AckA) with citrate bound at the dimeric interface

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
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE CIT A 501
ChainResidue
AARG178
AHOH478
AHOH538
AHOH620
BARG309
BLYS312
BHOH552
BHOH608
AASP257
ATHR258
ALEU259
AGLY260
ATYR313
AHOH422
AHOH452
AHOH470

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 601
ChainResidue
ATYR188
AGLN191
AGLU192
AGLN393

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 604
ChainResidue
AGLY367
ALYS368
ASER369

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 602
ChainResidue
BPHE187
BGLU192
BLYS195
BGLN393

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 603
ChainResidue
BVAL148
BPHE149
BPHE153
BTHR184
BPHE187
BASP394
BHOH415
BHOH420

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AASP150
BASP150

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AARG91
AHIS210
AASP285
AGLY333
AGLU387
BASN10
BLYS17
BARG91
BHIS210
BASP285
BGLY333
BGLU387
AASN10
ALYS17

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
BHIS182
AHIS182
AARG243
BARG243

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PDB entries from 2024-06-12

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