Structure of PDB 1e2e Chain A

Receptor sequence
>1e2eA (length=209) Species: 9606 (Homo sapiens) [Search protein sequence]
RRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLL
SSYLQKKSDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGV
AFTGAKENFSLDWCKQPDVGLPKPDLVLFLQLQLADAAKRGAFGHERYEN
GAFQERALRCFHQLMKDTTLNWKMVDASKSIEAVHEDIRVLSEDAIATAT
EKPLGELWK
3D structure
PDB1e2e Insights Into the Phosphoryltransfer Mechanism of Human Thymidylate Kinase Gained from Crystal Structures of Enzyme Complexes Along the Reaction Coordinate
ChainA
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.4.9: dTMP kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 TMP A F42 F72 R76 R97 G102 F105 Y151 F39 F69 R73 R94 G99 F102 Y148
BS02 ADP A R16 A17 G18 K19 S20 T21 R143 I184 R13 A14 G15 K16 S17 T18 R140 I181
BS03 AF3 A D15 R16 K19 R97 D12 R13 K16 R94
Gene Ontology
Molecular Function
GO:0004550 nucleoside diphosphate kinase activity
GO:0004798 thymidylate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006227 dUDP biosynthetic process
GO:0006233 dTDP biosynthetic process
GO:0006235 dTTP biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
GO:0043627 response to estrogen
GO:0045445 myoblast differentiation
GO:0046105 thymidine biosynthetic process
GO:0046686 response to cadmium ion
GO:0046940 nucleoside monophosphate phosphorylation
GO:0071363 cellular response to growth factor stimulus
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005829 cytosol

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Molecular Function

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Cellular Component
External links
PDB RCSB:1e2e, PDBe:1e2e, PDBj:1e2e
PDBsum1e2e
PubMed10873853
UniProtP23919|KTHY_HUMAN Thymidylate kinase (Gene Name=DTYMK)

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