Structure of PDB 1h72 Chain C

Receptor sequence
>1h72C (length=296) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MKVRVKAPCTSANLGVGFDVFGLCLKEPYDVIEVEAIDDKEIIIEVDDKN
IPTDPDKNVAGIVAKKMIDDFNIGKGVKITIKKGVKAGSGLGSSAASSAG
TAYAINELFKLNLDKLKLVDYASYGELASSGAKHADNVAPAIFGGFTMVT
NYEPLEVLHIPIDFKLDILIAIPNISINTKEAREILPKAVGLKDLVNNVG
KACGMVYALYNKDKSLFGRYMMSDKVIEPVRGKLIPNYFKIKEEVKDKVY
GITISGSGPSIIAFPKEEFIDEVENILRDYYENTIRTEVGKGVEVV
3D structure
PDB1h72 Structural Basis for the Catalysis and Substrate Specificity of Homoserine Kinase
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E130 T183
Catalytic site (residue number reindexed from 1) E126 T179
Enzyme Commision number 2.7.1.39: homoserine 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 HSE C N17 F22 D23 D140 N141 R187 R235 N13 F18 D19 D136 N137 R183 R231
BS02 ANP C I55 N62 V63 K87 A91 G92 G94 L95 G96 S97 S98 S101 S133 T183 S261 I51 N58 V59 K83 A87 G88 G90 L91 G92 S93 S94 S97 S129 T179 S257
Gene Ontology
Molecular Function
GO:0004413 homoserine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006566 threonine metabolic process
GO:0009088 threonine biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h72, PDBe:1h72, PDBj:1h72
PDBsum1h72
PubMed11535056
UniProtQ58504|KHSE_METJA Homoserine kinase (Gene Name=thrB)

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