2X7K
The crystal structure of PPIL1 in complex with cyclosporine A suggests a binding mode for SKIP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000398 | biological_process | mRNA splicing, via spliceosome |
| A | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005681 | cellular_component | spliceosomal complex |
| A | 0005730 | cellular_component | nucleolus |
| A | 0006397 | biological_process | mRNA processing |
| A | 0006457 | biological_process | protein folding |
| A | 0008380 | biological_process | RNA splicing |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0071006 | cellular_component | U2-type catalytic step 1 spliceosome |
| A | 0071007 | cellular_component | U2-type catalytic step 2 spliceosome |
| A | 0071013 | cellular_component | catalytic step 2 spliceosome |
| A | 0071014 | cellular_component | post-mRNA release spliceosomal complex |
| A | 0071020 | cellular_component | post-spliceosomal complex |
| A | 0097718 | molecular_function | disordered domain specific binding |
| A | 1990403 | biological_process | embryonic brain development |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 1167 |
| Chain | Residue |
| A | HIS31 |
| A | ASP89 |
| A | CYS133 |
| A | HOH2087 |
| A | HOH2190 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 1168 |
| Chain | Residue |
| A | GLU26 |
| A | HIS87 |
| A | CYS133 |
| A | HOH2239 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 1169 |
| Chain | Residue |
| A | ASP7 |
| A | HOH2267 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR CHAIN B OF CYCLOSPORIN A |
| Chain | Residue |
| A | GLU17 |
| A | ARG55 |
| A | PHE60 |
| A | GLN63 |
| A | GLY71 |
| A | ALA101 |
| A | ASN102 |
| A | GLN111 |
| A | PHE113 |
| A | TRP121 |
| A | HIS126 |
| A | MET144 |
| A | HOH2032 |
| A | HOH2033 |
| A | HOH2066 |
| A | HOH2137 |
| A | HOH2161 |
| B | HOH2001 |
| B | HOH2002 |
| B | HOH2003 |
| B | HOH2004 |
| B | HOH2005 |
| B | HOH2006 |
| B | HOH2007 |
| B | HOH2008 |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YngTkFHRIIkdFMiQGG |
| Chain | Residue | Details |
| A | TYR48-GLY65 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 154 |
| Details | Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16595688","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
