Structure of PDB 1tid Chain A

Receptor sequence

>1tidA (length=136) Species: 1422 (Geobacillus stearothermophilus)

MRNEMHLQFSARSENESFARVTVAAFVAQLDPTMDELTEIKTVVSEAVTN
AIIHGYNNDPNGIVSISVIIEDGVVHLTVRDEGVGIPDIEEARQPLFTTK
PELERSGMGFTIMENFMDEVIVESEVNKGTTVYLKK

3D structure

• PDB: 1tid 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: 2.5 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	ATP	A	N50 H54 D81 V84 G85 I86 F97 T98 T99 R105 S106 G107 M108 G109 F110 T130	N50 H54 D81 V84 G85 I86 F97 T98 T99 R105 S106 G107 M108 G109 F110 T130

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