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4IJN

Crystal structure of an acetate kinase from Mycobacterium smegmatis bound to AMP and sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006082biological_processorganic acid metabolic process
A0006083biological_processacetate 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
B0006083biological_processacetate 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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG72
AHIS104
AHIS161
AGLY193
AARG222
AEDO404
AHOH811
AHOH826

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP A 402
ChainResidue
AASN192
AASP263
APHE264
AARG265
AALA310
AGLY311
AVAL312
AASN315
AVAL316
AHOH701
AHOH811
AHOH824
AGLY191

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AGLU181
ASER182
AASN184
AALA200
AGLY201
AARG302
AHOH776

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AARG72
AVAL74
AHIS104
AASP129
APHE160
AHIS161
AMET209
AARG222
ASO4401

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
BARG72
BHIS104
BHIS161
BGLY193
BARG222
BEDO403
BHOH782
BHOH784
BHOH820

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AMP B 402
ChainResidue
BGLY191
BASN192
BASP263
BPHE264
BARG265
BALA310
BGLY311
BVAL312
BASN315
BVAL316
BHOH781
BHOH782
BHOH784
BHOH821

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BARG72
BVAL74
BHIS104
BPHE160
BHIS161
BMET209
BARG222
BSO4401

Functional Information from PROSITE/UniProt
site_idPS01075
Number of Residues12
DetailsACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvVNsGSSSlK
ChainResidueDetails
AVAL4-LYS15

site_idPS01076
Number of Residues18
DetailsACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. QIvlHlGnGaSAsAvagG
ChainResidueDetails
AGLN185-GLY202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AASP129
BASP129

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
AARG72
AGLU365
BASN8
BLYS15
BARG72
BGLU365
AASN8
ALYS15

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
BASP263
BGLY311
AHIS189
AASP263
AGLY311
BHIS189

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00020
ChainResidueDetails
BHIS161
BARG222
AHIS161
AARG222

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PDB entries from 2024-06-12

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