Structure of PDB 5djk Chain A

Receptor sequence

>5djkA (length=251) Species: 1773 (Mycobacterium tuberculosis)

DLTDAELAADLAADAGKLLLQVRAEIGFDQPWTLGEAGDRQANSLLLRRL
QAERPGDAVLSEEAHDDLARLKSDRVWIIDPLDGTREFSTPGRDDWAVHI
ALWRRPEITDAAVALPARGNVVYRTDTVTSGAAPAGVPGTLRIAVSATRP
PAVLHRIRQTLAIQPVSIGSAGAKAMAVIDGYVDAYLHAGGQWEWDSAAP
AGVMLAAGMHASRLDGSPLRYNQLDPYLPDLLMCRAEVAPILLGAIADAW
R

3D structure

• PDB: 5djk Crystal Structures of Mycobacterium tuberculosis CysQ, with Substrate and Products Bound.
• Chain: A
• Resolution: 1.799 Å

Enzymatic activity

• Enzyme Commision number: 3.1.3.11: fructose-bisphosphatase.
  3.1.3.25: inositol-phosphate phosphatase.
  3.1.3.7: 3'(2'),5'-bisphosphate nucleotidase.

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	CA	A	E73 D91 L93	E62 D80 L82
BS02	CA	A	D91 D94 D212	D80 D83 D196

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0005515 protein binding
• GO:0008441 3'(2'),5'-bisphosphate nucleotidase activity
• GO:0008934 inositol monophosphate 1-phosphatase activity
• GO:0016787 hydrolase activity
• GO:0030145 manganese ion binding
• GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
• GO:0046872 metal ion binding
• GO:0050897 cobalt ion binding
• GO:0052832 inositol monophosphate 3-phosphatase activity
• GO:0052833 inositol monophosphate 4-phosphatase activity
• GO:0052834 inositol monophosphate phosphatase activity

Biological Process

• GO:0000103 sulfate assimilation
• GO:0050427 3'-phosphoadenosine 5'-phosphosulfate metabolic process

Cellular Component

• GO:0005886 plasma membrane

External links

• PDB: RCSB:5djk, PDBe:5djk, PDBj:5djk
• PDBsum: 5djk
• PubMed: 26512869
• UniProt: P9WKJ1|CYSQ_MYCTU 3'-phosphoadenosine 5'-phosphate phosphatase (Gene Name=cysQ)