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1TUY

Acetate Kinase complexed with ADP, AlF3 and acetate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006082biological_processorganic acid metabolic process
A0006085biological_processacetyl-CoA biosynthetic process
A0008776molecular_functionacetate kinase activity
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006082biological_processorganic acid metabolic process
B0006085biological_processacetyl-CoA biosynthetic process
B0008776molecular_functionacetate kinase activity
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
AARG91
AHIS123
AHIS180
AGLY212
AARG241

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADP A 401
ChainResidue
APHE284
AARG285
AGLY331
AILE332
AASN335
ASER336
ALYS14
AGLY210
AASN211
AASP283

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP B 400
ChainResidue
BGLY210
BASN211
BASP283
BPHE284
BARG285
BALA330
BGLY331
BILE332
BASN335
BARG362
BAF3448
BHOH457

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE AF3 B 448
ChainResidue
BHIS180
BADP400
BACY425

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 425
ChainResidue
BVAL93
BHIS94
BARG241
BAF3448
BHOH450

Functional Information from PROSITE/UniProt
site_idPS01075
Number of Residues12
DetailsACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvINaGSSSlK
ChainResidueDetails
AVAL3-LYS14

site_idPS01076
Number of Residues18
DetailsACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. IItcHlGnGsSItAvegG
ChainResidueDetails
AILE204-GLY221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:11133963, ECO:0000269|PubMed:15647264
ChainResidueDetails
AASP148
BASP148

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASN7
AGLU384
BASN7
BGLU384

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ALYS14
BGLY331
AARG91
AHIS208
AASP283
AGLY331
BLYS14
BARG91
BHIS208
BASP283

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AHIS180
AARG241
BHIS180
BARG241

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1g99
ChainResidueDetails
AGLY212
ASER10
AASP148
AARG91
AARG241

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1g99
ChainResidueDetails
BGLY212
BSER10
BASP148
BARG91
BARG241

site_idMCSA1
Number of Residues5
DetailsM-CSA 643
ChainResidueDetails
AASN7metal ligand
AARG91electrostatic stabiliser, polar interaction
AHIS180electrostatic stabiliser, polar interaction
AARG241electrostatic stabiliser, polar interaction
AGLU384metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 643
ChainResidueDetails
BASN7metal ligand
BARG91electrostatic stabiliser, polar interaction
BHIS180electrostatic stabiliser, polar interaction
BARG241electrostatic stabiliser, polar interaction
BGLU384metal ligand

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PDB entries from 2024-07-24

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