Structure of PDB 1h74 Chain D

Receptor sequence
>1h74D (length=296) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MKVRVKAPCTSANLGVGFDVFGLCLKEPYDVIEVEAIDDKEIIIEVDDKN
IPTDPDKNVAGIVAKKMIDDFNIGKGVKITIKKGVKAGSGLGSSAASSAG
TAYAINELFKLNLDKLKLVDYASYGELASSGAKHADNVAPAIFGGFTMVT
NYEPLEVLHIPIDFKLDILIAIPNISINTKEAREILPKAVGLKDLVNNVG
KACGMVYALYNKDKSLFGRYMMSDKVIEPVRGKLIPNYFKIKEEVKDKVY
GITISGSGPSIIAFPKEEFIDEVENILRDYYENTIRTEVGKGVEVV
3D structure
PDB1h74 Structural Basis for the Catalysis and Substrate Specificity of Homoserine Kinase
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ILE D N17 F22 D23 R187 R235 N13 F18 D19 R183 R231
BS02 AGS D I55 N62 V63 K87 G94 L95 G96 S97 S98 S101 S133 N141 T183 S261 I51 N58 V59 K83 G90 L91 G92 S93 S94 S97 S129 N137 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1h74, PDBe:1h74, PDBj:1h74
PDBsum1h74
PubMed11535056
UniProtQ58504|KHSE_METJA Homoserine kinase (Gene Name=thrB)

[Back to BioLiP]