Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KIM

CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE I COMPLEXED WITH DEOXYTHYMIDINE

Replaces:  1KIN
Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004797molecular_functionthymidine kinase activity
A0005524molecular_functionATP binding
A0006230biological_processTMP biosynthetic process
A0009157biological_processdeoxyribonucleoside monophosphate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0071897biological_processDNA biosynthetic process
B0000166molecular_functionnucleotide binding
B0004797molecular_functionthymidine kinase activity
B0005524molecular_functionATP binding
B0006230biological_processTMP biosynthetic process
B0009157biological_processdeoxyribonucleoside monophosphate biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0071897biological_processDNA biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
AHIS58
AGLY59
AMET60
AGLY61
ALYS62
ATHR63
AARG222
AHOH409
AHOH442

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 4
ChainResidue
BHIS58
BGLY59
BMET60
BGLY61
BLYS62
BTHR63
BARG222
BHOH410
BHOH441

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE THM A 1
ChainResidue
AHIS58
AGLU83
AILE97
AILE100
ATYR101
AGLN125
AARG163
AALA168
ATYR172
AARG222
AGLU225
AHOH408
AHOH409
AHOH410

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE THM B 2
ChainResidue
BHIS58
BGLU83
BTYR101
BGLN125
BMET128
BALA168
BTYR172
BGLU225
BHOH409
BHOH410
BHOH411
BHOH484

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04029
ChainResidueDetails
AGLU83
BGLU83

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04029
ChainResidueDetails
AGLY56
BARG222
ATYR101
AGLN125
AARG216
AARG222
BGLY56
BTYR101
BGLN125
BARG216

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 11262392, 9715911, 9336833
ChainResidueDetails
AGLU83
AARG222
AARG220
AARG163
ALYS62
AGLU225

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon