Structure of PDB 1til Chain A

Receptor sequence

>1tilA (length=141) Species: 1422 (Geobacillus stearothermophilus)

MRNEMHLQFSARSENESFARVTVAAFVAQLDPTMDELTEIKTVVSEAVTN
AIIHGYNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEARQPLFTTK
PELERSGMGFTIMENFMDEVIVESEVNKGTTVYLKKHIVKS

3D structure

• PDB: 1til Crystal Structures of the ADP and ATP Bound Forms of the Bacillus Anti-sigma Factor SpoIIAB in Complex with the Anti-anti-sigma SpoIIAA.
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E46 N50 R105
• Catalytic site (residue number reindexed from 1): E46 N50 R105
• Enzyme Commision number: 2.7.11.1: non-specific serine/threonine protein 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	MG	A	E46 N50	E46 N50
BS02	ATP	A	N50 H54 G55 I86 A92 T98 T99 R105 S106 G107 M108 G109 F110	N50 H54 G55 I86 A92 T98 T99 R105 S106 G107 M108 G109 F110

Gene Ontology

Molecular Function

• GO:0004672 protein kinase activity
• GO:0004674 protein serine/threonine kinase activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016989 sigma factor antagonist activity
• GO:0044024 histone H2AS1 kinase activity
• GO:0106310 protein serine kinase activity

Biological Process

• GO:0006338 chromatin remodeling
• GO:0006468 protein phosphorylation
• GO:0010468 regulation of gene expression
• GO:0016310 phosphorylation
• GO:0030435 sporulation resulting in formation of a cellular spore
• GO:0030436 asexual sporulation
• GO:0042174 negative regulation of sporulation resulting in formation of a cellular spore
• GO:0045892 negative regulation of DNA-templated transcription

External links

• PDB: RCSB:1til, PDBe:1til, PDBj:1til
• PDBsum: 1til
• PubMed: 15236958
• UniProt: O32727|SP2AB_GEOSE Anti-sigma F factor (Gene Name=spoIIAB)