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

4JBX

Crystal structure of thymidine kinase from Herpes simplex virus type 1 in complex with SK-78

Functional Information from GO Data
ChainGOidnamespacecontents
A0004797molecular_functionthymidine kinase activity
A0005524molecular_functionATP binding
A0006230biological_processTMP biosynthetic process
B0004797molecular_functionthymidine kinase activity
B0005524molecular_functionATP binding
B0006230biological_processTMP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SK7 A 601
ChainResidue
AHIS58
ATYR172
AARG222
AHOH725
AHOH745
AGLU83
ATRP88
AILE97
AILE100
AGLN125
AMET128
AARG163
AALA168

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AHIS58
AGLY59
AARG220
AARG222
AHOH731
AHOH853

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AHIS105
AARG106
AARG226
BSER74
BARG75

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ALYS62
AARG212
AARG216
BARG220

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SK7 B 401
ChainResidue
BHIS58
BGLU83
BTRP88
BILE97
BTYR101
BGLN125
BMET128
BARG163
BTYR172
BHOH565
BHOH607

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
BHIS58
BGLY59
BMET60
BGLY61
BLYS62
BTHR63
BARG216
BHOH548
BHOH579
BHOH607

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BLYS317
BARG320
BHOH507

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 404
ChainResidue
BLYS219
BARG220

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 405
ChainResidue
ALEU229
BARG337

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_idMCSA1
Number of Residues7
DetailsM-CSA 588
ChainResidueDetails
ALYS62electrostatic stabiliser, polar interaction
AGLU83proton acceptor, proton donor
AASP162metal ligand
AARG163electrostatic stabiliser, polar interaction
AARG220electrostatic stabiliser, polar interaction
AARG222electrostatic stabiliser, polar interaction
AGLU225electrostatic stabiliser, polar interaction

site_idMCSA2
Number of Residues5
DetailsM-CSA 588
ChainResidueDetails
BLYS62electrostatic stabiliser, polar interaction
BGLU83proton acceptor, proton donor
BASP162metal ligand
BARG163electrostatic stabiliser, polar interaction
BARG220electrostatic stabiliser, polar interaction

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon