Structure of PDB 5x5h Chain A

Receptor sequence

>5x5hA (length=385) Species: 196627 (Corynebacterium glutamicum ATCC 13032)

FDPNTQGFSTASIHAGYEPDDYYGSINTPIYASTTFAQNAPNELRKGYEY
TRVGNPTIVALEQTVAALEGAKYGRAFSSGMAATDILFRIILKPGDHIVL
GNDAYGGTYRLIDTVFTAWGVEYTVVDTSVVEEVKAAIKDNTKLIWVETP
TNPALGITDIEAVAKLTEGTNAKLVVDNTFASPYLQQPLKLGAHAVLHST
TKYIGGHSDVVGGLVVTNDQEMDEELLFMQGGIGPIPSVFDAYLTARGLK
TLAVRMDRHCDNAEKIAEFLDSRPEVSTVLYPGLKNHPGHEVAAKQMKRF
GGMISVRFAGGEEAAKKFCTSTKLICLAESLGGVESLLEHPATMTHQSAA
GSQLEVPRDLVRISIGIEDIEDLLADVEQALNNLH

3D structure

• PDB: 5x5h Structural Insights into Substrate Specificity of Cystathionine gamma-Synthase from Corynebacterium glutamicum
• Chain: A
• Resolution: 1.51 Å

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.

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	PLP	A	G82 M83 Y107 D179 S201 T203 K204	G80 M81 Y105 D177 S199 T201 K202
BS02	MG	A	E71 Q189 P190 L191	E69 Q187 P188 L189
BS03	MG	A	F38 Q40 E51	F36 Q38 E49

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

External links

• PDB: RCSB:5x5h, PDBe:5x5h, PDBj:5x5h
• PDBsum: 5x5h
• PubMed: 28675039
• UniProt: Q79VD9