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6C9R

Mycobacterium tuberculosis adenosine kinase bound to (2R,3S,4R,5R)-2-(hydroxymethyl)-5-(6-(thiophen-3-yl)-9H-purin-9-yl)tetrahydrofuran-3,4-diol

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
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
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
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0032567molecular_functiondGTP binding
B0044209biological_processAMP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ERJ A 401
ChainResidue
ASER8
AARG176
AGLY254
AASP257
AHOH505
AHOH563
AHOH572
BSER36
AALA10
AASP12
AGLY47
AGLY48
AVAL49
AASN52
APHE102
APHE116

site_idAC2
Number of Residues8
Detailsbinding site for residue ERJ A 402
ChainResidue
APHE-3
AGLY225
APRO226
AVAL243
AVAL244
AGLU246
AVAL255
AHOH577

site_idAC3
Number of Residues4
Detailsbinding site for residue NA A 403
ChainResidue
AASP251
AVAL287
ASER290
AGLY292

site_idAC4
Number of Residues17
Detailsbinding site for residue ERJ B 401
ChainResidue
ASER36
BSER8
BALA10
BASP12
BGLY47
BGLY48
BVAL49
BASN52
BPHE102
BPHE116
BGLN172
BARG176
BASP257
BHOH510
BHOH531
BHOH565
BHOH570

site_idAC5
Number of Residues6
Detailsbinding site for residue ERJ B 402
ChainResidue
BGLY137
BPRO226
BVAL244
BGLU246
BGLN249
BHOH553

site_idAC6
Number of Residues5
Detailsbinding site for residue NA B 403
ChainResidue
BASP251
BTHR253
BVAL287
BSER290
BGLY292

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL B 404
ChainResidue
ATHR105
AILE113
BTHR105
BILE113

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
ASER8
BASP12
BGLY48
BASN52
BPHE102
BPHE116
BGLN172
BASP257
AASP12
AGLY48
AASN52
APHE102
APHE116
AGLN172
AASP257
BSER8

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 2024-07-17

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