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2PKK

Crystal structure of M tuberculosis Adenosine Kinase complexed with 2-fluro adenosine

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
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2FA A 501
ChainResidue
ASER8
AMET121
AALA146
AASN147
AGLN172
AGLN173
AASP257
AHOH511
AASP12
ASER36
AGLY47
AGLY48
AVAL49
AASN52
APHE102
APHE116

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17597075
ChainResidueDetails
AASP257

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: in other chain => ECO:0000305|PubMed:17597075, ECO:0007744|PDB:2PKM
ChainResidueDetails
ASER8
AASP12
AGLY48
AASN52
APHE102
APHE116
AGLN172
AASP257

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0007744|PDB:2PKM
ChainResidueDetails
ASER36

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0000305|PubMed:25259627, ECO:0007744|PDB:4O1G
ChainResidueDetails
AASN195

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17597075, ECO:0000305|PubMed:25259627, ECO:0007744|PDB:2PKN, ECO:0007744|PDB:4O1G
ChainResidueDetails
ATHR223

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:25259627, ECO:0007744|PDB:4O1G
ChainResidueDetails
AGLY256

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ATHR2

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
AGLY254
AASP257
AVAL255
AGLY256

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PDB entries from 2024-07-24

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