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2ABS

Crystal structure of T. gondii adenosine kinase complexed with AMP-PCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004001molecular_functionadenosine kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006144biological_processpurine nucleobase metabolic process
A0006166biological_processpurine ribonucleoside salvage
A0016301molecular_functionkinase activity
A0034654biological_processnucleobase-containing compound biosynthetic process
A0044209biological_processAMP salvage
A0046872molecular_functionmetal ion binding
A0055086biological_processnucleobase-containing small molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1002
ChainResidue
AASN20
AALA71
ATHR167

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1003
ChainResidue
AVAL348
AHIS351
AGLY353
AHOH3038
AHOH3057

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ACP A 1001
ChainResidue
ATHR278
AARG279
AGLY280
AHIS281
AVAL284
AVAL302
AVAL305
AILE310
ATHR313
AASN314
AALA316
AGLY317
AASN342
AALA345
AHOH3033
AHOH3044
AHOH3076
AHOH3155
AHOH3159
AHOH3164
AHOH3248
AHOH3364
AHOH3400
AHOH3426
AHOH5466
AHOH5577
AASN223

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTnGAGDafvGGFL
ChainResidueDetails
AASP312-LEU325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
AASP318

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AALA185
AILE188
AALA191

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AARG136
AASP318

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AALA316
AGLY317
AGLY315
AASP318

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AGLY315
AARG261

site_idMCSA1
Number of Residues2
DetailsM-CSA 209
ChainResidueDetails
AARG136electrostatic stabiliser, hydrogen bond donor
AASP318hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

221716

PDB entries from 2024-06-26

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