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6C9N

Mycobacterium tuberculosis adenosine kinase bound to sangivamycin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004001molecular_functionadenosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005886cellular_componentplasma membrane
A0006166biological_processpurine ribonucleoside salvage
A0016301molecular_functionkinase activity
A0032567molecular_functiondGTP binding
A0044209biological_processAMP salvage
B0000287molecular_functionmagnesium ion binding
B0004001molecular_functionadenosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005886cellular_componentplasma membrane
B0006166biological_processpurine ribonucleoside salvage
B0016301molecular_functionkinase activity
B0032567molecular_functiondGTP binding
B0044209biological_processAMP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue SGV A 401
ChainResidue
ASER8
AALA146
AGLN172
AGLN173
AASP257
AHOH552
BSER36
AALA10
AASP12
AGLY47
AGLY48
AVAL49
AASN52
APHE102
APHE116

site_idAC2
Number of Residues7
Detailsbinding site for residue SGV A 402
ChainResidue
AGLY225
AVAL243
AGLU246
AGLN249
AVAL255
ALEU288
AHOH579

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 403
ChainResidue
ACYS104
ATHR105
AILE113
AALA114
ASER115
BTHR103
BTHR105
BILE113

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 404
ChainResidue
AASN195
ATHR223
AGLY256
AHOH501

site_idAC5
Number of Residues6
Detailsbinding site for residue NA A 405
ChainResidue
AASP251
ATHR253
AVAL287
ASER290
ATHR291
AGLY292

site_idAC6
Number of Residues15
Detailsbinding site for residue SGV B 401
ChainResidue
ASER36
BSER8
BALA10
BASP12
BGLY47
BGLY48
BVAL49
BASN52
BPHE102
BPHE116
BALA146
BGLN172
BGLN173
BASP257
BHOH550

site_idAC7
Number of Residues10
Detailsbinding site for residue SGV B 402
ChainResidue
BGLY225
BVAL243
BVAL244
BGLU246
BGLN249
BVAL255
BLEU288
BHOH558
BHOH566
BHOH575

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 B 403
ChainResidue
BASN195
BGLY256
BHOH505

site_idAC9
Number of Residues6
Detailsbinding site for residue NA B 404
ChainResidue
BASP251
BTHR253
BVAL287
BSER290
BTHR291
BGLY292

Functional Information from PROSITE/UniProt
site_idPS00583
Number of Residues25
DetailsPFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGvAgNMAfaIgVLGgevalvgaaG
ChainResidueDetails
AGLY47-GLY71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17597075
ChainResidueDetails
AASP257
BASP257

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: in other chain => ECO:0000305|PubMed:17597075, ECO:0007744|PDB:2PKM
ChainResidueDetails
AGLY48
AASN52
APHE102
APHE116
AGLN172
AASP257
BSER8
BASP12
BGLY48
BASN52
BPHE102
BPHE116
BGLN172
BASP257
ASER8
AASP12

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0007744|PDB:2PKM
ChainResidueDetails
ASER36
BSER36

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0000305|PubMed:25259627, ECO:0007744|PDB:4O1G
ChainResidueDetails
AASN195
BASN195

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0000305|PubMed:25259627, ECO:0007744|PDB:2PKN, ECO:0007744|PDB:4O1G
ChainResidueDetails
ATHR223
BTHR223

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:25259627, ECO:0007744|PDB:4O1G
ChainResidueDetails
AGLY256
BGLY256

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2
BTHR2

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PDB entries from 2024-06-12

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