Structure of PDB 1fwk Chain A

Receptor sequence
>1fwkA (length=296) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MKVRVKAPCTSANLGVGFDVFGLCLKEPYDVIEVEAIDDKEIIIEVDDKN
IPTDPDKNVAGIVAKKMIDDFNIGKGVKITIKKGVKAGSGLGSSAASSAG
TAYAINELFKLNLDKLKLVDYASYGELASSGAKHADNVAPAIFGGFTMVT
NYEPLEVLHIPIDFKLDILIAIPNISINTKEAREILPKAVGLKDLVNNVG
KACGMVYALYNKDKSLFGRYMMSDKVIEPVRGKLIPNYFKIKEEVKDKVY
GITISGSGPSIIAFPKEEFIDEVENILRDYYENTIRTEVGKGVEVV
3D structure
PDB1fwk Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily.
ChainA
Resolution2.1 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 ADP A I55 N62 V63 K87 S97 S98 S101 I51 N58 V59 K83 S93 S94 S97
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:1fwk, PDBe:1fwk, PDBj:1fwk
PDBsum1fwk
PubMed11188689
UniProtQ58504|KHSE_METJA Homoserine kinase (Gene Name=thrB)

[Back to BioLiP]