4MSP
Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifs
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 201 |
| Chain | Residue |
| A | ASP129 |
| A | ASN131 |
| A | ASP133 |
| A | LYS135 |
| A | GLU140 |
| A | HOH345 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 202 |
| Chain | Residue |
| A | PHE179 |
| A | GLU184 |
| A | HOH358 |
| A | ASP173 |
| A | ASP175 |
| A | ASP177 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 203 |
| Chain | Residue |
| A | GLU172 |
| A | GLU184 |
| A | TYR187 |
| A | HIS189 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE A 204 |
| Chain | Residue |
| A | LEU145 |
| A | HIS152 |
| A | PGO206 |
| B | LEU145 |
| B | GLU148 |
| B | HIS152 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE A 205 |
| Chain | Residue |
| A | ALA89 |
| A | GLY93 |
| A | LYS94 |
| A | GLU95 |
| A | GLU103 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGO A 206 |
| Chain | Residue |
| A | HIS152 |
| A | GLY153 |
| A | ALA154 |
| A | 1PE204 |
| B | LYS188 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGO A 207 |
| Chain | Residue |
| A | PRO16 |
| A | PHE17 |
| A | CYS19 |
| B | ASP132 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGO A 208 |
| Chain | Residue |
| A | HIS32 |
| A | TYR33 |
| A | HIS48 |
| A | LYS81 |
| A | ASN109 |
| A | HOH383 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 201 |
| Chain | Residue |
| B | ASP129 |
| B | ASN131 |
| B | ASP133 |
| B | LYS135 |
| B | GLU140 |
| B | HOH308 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 202 |
| Chain | Residue |
| B | ASP173 |
| B | ASP175 |
| B | ASP177 |
| B | PHE179 |
| B | GLU184 |
| B | HOH428 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGO B 203 |
| Chain | Residue |
| A | ARG120 |
| A | SER124 |
| A | PHE185 |
| B | HIS152 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGO B 204 |
| Chain | Residue |
| A | TRP57 |
| A | ARG116 |
| B | ILE115 |
| B | HOH316 |
| B | HOH392 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PGO B 205 |
| Chain | Residue |
| B | HIS20 |
| B | HOH338 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PGO B 206 |
| Chain | Residue |
| B | VAL12 |
| B | HOH423 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGO B 207 |
| Chain | Residue |
| A | ILE56 |
| A | TRP57 |
| A | HOH313 |
| A | HOH320 |
| B | LEU28 |
| B | TRP57 |
| B | ARG116 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 180 |
| Details | Domain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24272907","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24821723","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4MSP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24272907","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24821723","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4MSP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
