Structure of PDB 5x5h Chain A Binding Site BS03
Receptor Information
>5x5h Chain A (length=385) Species:
196627
(Corynebacterium glutamicum ATCC 13032) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
FDPNTQGFSTASIHAGYEPDDYYGSINTPIYASTTFAQNAPNELRKGYEY
TRVGNPTIVALEQTVAALEGAKYGRAFSSGMAATDILFRIILKPGDHIVL
GNDAYGGTYRLIDTVFTAWGVEYTVVDTSVVEEVKAAIKDNTKLIWVETP
TNPALGITDIEAVAKLTEGTNAKLVVDNTFASPYLQQPLKLGAHAVLHST
TKYIGGHSDVVGGLVVTNDQEMDEELLFMQGGIGPIPSVFDAYLTARGLK
TLAVRMDRHCDNAEKIAEFLDSRPEVSTVLYPGLKNHPGHEVAAKQMKRF
GGMISVRFAGGEEAAKKFCTSTKLICLAESLGGVESLLEHPATMTHQSAA
GSQLEVPRDLVRISIGIEDIEDLLADVEQALNNLH
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5x5h Chain A Residue 406 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
5x5h
Structural Insights into Substrate Specificity of Cystathionine gamma-Synthase from Corynebacterium glutamicum
Resolution
1.51 Å
Binding residue
(original residue number in PDB)
F38 Q40 E51
Binding residue
(residue number reindexed from 1)
F36 Q38 E49
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
R54 Y107 D179 K204
Catalytic site (residue number reindexed from 1)
R52 Y105 D177 K202
Enzyme Commision number
2.5.1.48
: cystathionine gamma-synthase.
Gene Ontology
Molecular Function
GO:0003962
cystathionine gamma-synthase activity
GO:0016740
transferase activity
GO:0016846
carbon-sulfur lyase activity
GO:0030170
pyridoxal phosphate binding
GO:0046872
metal ion binding
Biological Process
GO:0009086
methionine biosynthetic process
GO:0019346
transsulfuration
Cellular Component
GO:0005737
cytoplasm
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:5x5h
,
PDBe:5x5h
,
PDBj:5x5h
PDBsum
5x5h
PubMed
28675039
UniProt
Q79VD9
[
Back to BioLiP
]