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5FUY

catalytic domain of Thymidine kinase from Trypanosoma brucei with dTMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004797molecular_functionthymidine kinase activity
A0005524molecular_functionATP binding
B0004797molecular_functionthymidine kinase activity
B0005524molecular_functionATP binding
C0004797molecular_functionthymidine kinase activity
C0005524molecular_functionATP binding
D0004797molecular_functionthymidine kinase activity
D0005524molecular_functionATP binding
E0004797molecular_functionthymidine kinase activity
E0005524molecular_functionATP binding
F0004797molecular_functionthymidine kinase activity
F0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 1384
ChainResidue
BPHE215
BALA216
BGLY217
BLYS218
BTHR219
BQBT1385
BHOH2002
BHOH2007

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1385
ChainResidue
APHE215
AALA216
AGLY217
ALYS218
ATHR219
AQBT1386
AHOH2008
APRO213

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 E 1386
ChainResidue
EPRO213
EPHE215
EALA216
EGLY217
ELYS218
ETHR219
EQBT1387

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 F 1385
ChainResidue
FPRO213
FPHE215
FALA216
FGLY217
FLYS218
FTHR219
FQBT1386

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 D 1383
ChainResidue
DPHE215
DALA216
DGLY217
DLYS218
DTHR219
DQBT1384

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C 1385
ChainResidue
CMET214
CPHE215
CALA216
CGLY217
CLYS218
CTHR219
CQBT1386

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE QBT B 1385
ChainResidue
BMET214
BLYS218
BGLU286
BGLN288
BPHE289
BLEU312
BASP315
BTYR316
BTHR352
BARG361
BLYS362
BLEU363
BVAL364
BGLY365
BTYR370
BPO41384

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE QBT A 1386
ChainResidue
AMET214
ALYS218
AGLU286
AGLN288
APHE289
ALEU312
AASP315
ATYR316
ATHR352
AARG361
ALYS362
ALEU363
AVAL364
AGLY365
ATYR370
APO41385

site_idAC9
Number of Residues16
DetailsBINDING SITE FOR RESIDUE QBT E 1387
ChainResidue
EMET214
ELYS218
EGLU286
EGLN288
EPHE289
ELEU312
EASP315
ETYR316
ETHR352
EARG361
ELYS362
ELEU363
EVAL364
EGLY365
ETYR370
EPO41386

site_idBC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE QBT F 1386
ChainResidue
FTHR352
FARG361
FLYS362
FLEU363
FVAL364
FGLY365
FTYR370
FPO41385
FHOH2003
FMET214
FLYS218
FGLU286
FGLN288
FPHE289
FLEU312
FASP315
FTYR316

site_idBC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE QBT D 1384
ChainResidue
DMET214
DLYS218
DGLU286
DGLN288
DPHE289
DLEU312
DASP315
DTYR316
DTHR352
DARG361
DLYS362
DLEU363
DVAL364
DGLY365
DTYR370
DPO41383

site_idBC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE QBT C 1386
ChainResidue
CMET214
CLYS218
CTHR219
CGLU286
CGLN288
CPHE289
CLEU312
CASP315
CTYR316
CTHR352
CARG361
CLYS362
CLEU363
CVAL364
CGLY365
CTYR370
CPO41385

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1385
ChainResidue
DCYS341
DCYS344
DCYS374
DCYS377

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1386
ChainResidue
BCYS341
BCYS344
BCYS374
BCYS377

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1387
ChainResidue
CCYS341
CCYS344
CCYS374
CCYS377

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1387
ChainResidue
ACYS341
ACYS344
ACYS374
ACYS377

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1388
ChainResidue
ECYS341
ECYS344
ECYS374
ECYS377

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 1387
ChainResidue
FCYS341
FCYS344
FCYS374
FCYS377

Functional Information from PROSITE/UniProt
site_idPS00603
Number of Residues14
DetailsTK_CELLULAR_TYPE Thymidine kinase cellular-type signature. GgsDmYmSvCRsCY
ChainResidueDetails
AGLY365-TYR378

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PDB entries from 2024-07-24

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