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1E2N

HPT + HMTT

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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
AHIS58
AGLY59
ATHR64
ATHR65
AARG163
AARG220
AARG222
ARCA500

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 400
ChainResidue
BHIS58
BGLY59
BMET60
BGLY61
BLYS62
BTHR63
BHOH2078
BHOH2079
BHOH2080
ALYS219

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE RCA A 500
ChainResidue
AHIS58
AGLU83
AMET85
ATRP88
AILE97
AILE100
AGLN125
AMET128
ATYR132
AARG163
AALA167
AALA168
ATYR172
AARG222
ASO4400
AHOH2024
AHOH2027

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RCA B 500
ChainResidue
BHIS58
BGLU83
BMET85
BTRP88
BILE97
BILE100
BTYR101
BGLN125
BMET128
BARG163
BALA168
BTYR172
BHOH2081

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 Residues4
DetailsAnnotated By Reference To The Literature 1kim
ChainResidueDetails
AGLU83
AARG222
AGLY59
AARG163

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1kim
ChainResidueDetails
BGLU83
BGLY59
BARG163

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 Residues4
DetailsM-CSA 588
ChainResidueDetails
BLYS62electrostatic stabiliser, polar interaction
BGLU83proton acceptor, proton donor
BASP162metal ligand
BARG163electrostatic stabiliser, polar interaction

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PDB entries from 2025-06-11

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