Structure of PDB 3hyk Chain C

Receptor sequence
>3hykC (length=116) Species: 1392 (Bacillus anthracis) [Search protein sequence]
AMIVGIGIDIIELNRIEKMLDKFMERILTENERNVAKGLKGSRLTEFVAG
RFAAKEAYSKAVGTGIGKEVSFLDIEVRNDDRGKPILITSTEHIVHLSIS
HSKEFAVAQVVLESSS
3D structure
PDB3hyk Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
ChainC
Resolution2.31 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) K62 H103
Catalytic site (residue number reindexed from 1) K60 H101
Enzyme Commision number 2.7.8.7: holo-[acyl-carrier-protein] synthase.
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 A3P C E58 K62 G65 T66 E56 K60 G63 T64
BS02 MG C D8 E58 D9 E56
BS03 A3P C R14 M18 R15 M19
BS04 A3P C R45 R53 R84 G85 K86 P87 I101 S102 H103 R43 R51 R82 G83 K84 P85 I99 S100 H101
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008897 holo-[acyl-carrier-protein] synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3hyk, PDBe:3hyk, PDBj:3hyk
PDBsum3hyk
PubMed22993090
UniProtQ81JG3|ACPS_BACAN Holo-[acyl-carrier-protein] synthase (Gene Name=acpS)

[Back to BioLiP]