1TH8
Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: inhibitory complex with ADP, crystal form II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0010468 | biological_process | regulation of gene expression |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016989 | molecular_function | sigma factor antagonist activity |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0030436 | biological_process | asexual sporulation |
| A | 0042174 | biological_process | negative regulation of sporulation resulting in formation of a cellular spore |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0043856 | molecular_function | anti-sigma factor antagonist activity |
| B | 0045152 | molecular_function | antisigma factor binding |
| B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 602 |
| Chain | Residue |
| A | ASN50 |
| A | ADP200 |
| A | HOH636 |
| B | HOH149 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP A 200 |
| Chain | Residue |
| A | ILE86 |
| A | ALA92 |
| A | SER106 |
| A | GLY107 |
| A | GLY109 |
| A | PHE110 |
| A | THR130 |
| A | MG602 |
| A | HOH603 |
| A | HOH604 |
| A | HOH612 |
| A | HOH615 |
| A | HOH620 |
| A | HOH636 |
| B | HOH149 |
| A | ASN50 |
| A | ALA51 |
| A | HIS54 |
| A | GLY55 |
| A | ASP81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 110 |
| Details | Domain: {"description":"STAS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1l0o |
| Chain | Residue | Details |
| A | GLU46 | |
| A | ARG105 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 760 |
| Chain | Residue | Details |
| A | GLU46 | activator, electrostatic stabiliser, proton acceptor |
| A | ASN50 | metal ligand |
| A | ARG105 | electrostatic stabiliser, polar interaction |
