1C5F
CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A
Replaces: 1QTLFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| A | 0006457 | biological_process | protein folding |
| C | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| C | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| C | 0006457 | biological_process | protein folding |
| E | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| E | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| E | 0006457 | biological_process | protein folding |
| G | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| G | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| G | 0006457 | biological_process | protein folding |
| I | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| I | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| I | 0006457 | biological_process | protein folding |
| K | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| K | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| K | 0006457 | biological_process | protein folding |
| M | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| M | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| M | 0006457 | biological_process | protein folding |
| O | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| O | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| O | 0006457 | biological_process | protein folding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN B OF CYCLOSPORIN A |
| Chain | Residue |
| A | ARG66 |
| A | HIS132 |
| A | HIS137 |
| B | HOH2001 |
| A | PHE71 |
| A | GLN74 |
| A | GLY83 |
| A | ALA112 |
| A | ASN113 |
| A | LYS114 |
| A | GLN122 |
| A | PHE124 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR CHAIN D OF CYCLOSPORIN A |
| Chain | Residue |
| C | ARG66 |
| C | PHE71 |
| C | GLN74 |
| C | GLY83 |
| C | ALA112 |
| C | ASN113 |
| C | LYS114 |
| C | GLN122 |
| C | PHE124 |
| C | HIS132 |
| C | HIS137 |
| C | HOH2023 |
| D | HOH2001 |
| D | HOH2003 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN F OF CYCLOSPORIN A |
| Chain | Residue |
| E | ARG66 |
| E | PHE71 |
| E | GLN74 |
| E | GLY83 |
| E | ALA112 |
| E | ASN113 |
| E | LYS114 |
| E | GLN122 |
| E | PHE124 |
| E | HIS132 |
| E | HIS137 |
| F | HOH2001 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR CHAIN H OF CYCLOSPORIN A |
| Chain | Residue |
| E | MET46 |
| E | ALA47 |
| E | ILE89 |
| E | HOH2016 |
| G | ARG66 |
| G | PHE71 |
| G | GLN74 |
| G | GLY83 |
| G | ALA112 |
| G | ASN113 |
| G | LYS114 |
| G | GLN122 |
| G | PHE124 |
| G | HIS132 |
| G | HIS137 |
| H | HOH2001 |
| H | HOH2002 |
| O | HIS132 |
| O | ILE136 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN J OF CYCLOSPORIN A |
| Chain | Residue |
| I | ARG66 |
| I | PHE71 |
| I | GLN74 |
| I | GLY83 |
| I | ALA112 |
| I | ASN113 |
| I | LYS114 |
| I | GLN122 |
| I | PHE124 |
| I | HIS132 |
| I | HIS137 |
| J | HOH2002 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR CHAIN L OF CYCLOSPORIN A |
| Chain | Residue |
| C | MET46 |
| C | ALA47 |
| C | ILE89 |
| K | ARG66 |
| K | PHE71 |
| K | GLN74 |
| K | GLY83 |
| K | ALA112 |
| K | ASN113 |
| K | LYS114 |
| K | GLN122 |
| K | PHE124 |
| K | HIS132 |
| K | HIS137 |
| K | HOH2038 |
| L | HOH2002 |
| L | HOH2003 |
| M | HIS132 |
| M | ILE136 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR CHAIN N OF CYCLOSPORIN A |
| Chain | Residue |
| M | PHE124 |
| M | HIS132 |
| M | HIS137 |
| N | HOH2001 |
| C | ARG34 |
| K | HIS132 |
| K | ILE136 |
| M | ARG66 |
| M | PHE71 |
| M | GLN74 |
| M | GLY83 |
| M | ALA112 |
| M | ASN113 |
| M | LYS114 |
| M | GLN122 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR CHAIN P OF CYCLOSPORIN A |
| Chain | Residue |
| E | ARG34 |
| E | TYR90 |
| G | HIS132 |
| O | ARG66 |
| O | PHE71 |
| O | GLN74 |
| O | GLY83 |
| O | ALA112 |
| O | ASN113 |
| O | LYS114 |
| O | GLN122 |
| O | PHE124 |
| O | HIS132 |
| O | HIS137 |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIknFMiQGG |
| Chain | Residue | Details |
| A | TYR59-GLY76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1320 |
| Details | Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






