4I9Y
Structure of the C-terminal domain of Nup358
Functional 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 |
| B | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 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 |
| D | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| D | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| D | 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 |
| F | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| F | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| F | 0006457 | biological_process | protein folding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 201 |
| Chain | Residue |
| A | ARG55 |
| A | ALA101 |
| A | ASN102 |
| A | HIS126 |
| A | HOH389 |
| A | HOH412 |
| A | HOH564 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | ASN27 |
| A | HOH382 |
| A | HIS0 |
| A | THR2 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 203 |
| Chain | Residue |
| A | HIS0 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TLA A 204 |
| Chain | Residue |
| A | PRO-1 |
| A | PHE25 |
| A | ILE28 |
| A | VAL90 |
| A | HOH310 |
| A | HOH316 |
| A | HOH516 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 205 |
| Chain | Residue |
| A | PRO-1 |
| A | HIS0 |
| A | MET1 |
| A | GLU23 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 201 |
| Chain | Residue |
| B | ARG55 |
| B | PHE60 |
| B | GLN63 |
| B | ALA101 |
| B | VAL113 |
| B | HIS126 |
| B | HOH337 |
| B | HOH357 |
| B | HOH441 |
| B | HOH452 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 202 |
| Chain | Residue |
| B | LYS91 |
| B | PHE124 |
| B | HOH346 |
| B | HOH366 |
| B | HOH388 |
| B | HOH401 |
| B | HOH548 |
| D | LYS91 |
| D | PHE124 |
| D | HOH395 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 203 |
| Chain | Residue |
| B | GLY45 |
| B | HOH365 |
| B | HOH447 |
| B | HOH508 |
| F | GLU86 |
| F | PHE88 |
| F | HOH354 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 204 |
| Chain | Residue |
| B | HIS0 |
| B | THR2 |
| B | ASN27 |
| B | HOH336 |
| B | HOH437 |
| B | HOH465 |
| D | PRO95 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 205 |
| Chain | Residue |
| B | HIS0 |
| B | HOH421 |
| D | PRO95 |
| D | HOH318 |
| D | HOH433 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TLA B 206 |
| Chain | Residue |
| B | PRO-1 |
| B | PHE25 |
| B | ILE28 |
| B | VAL90 |
| B | HOH311 |
| B | HOH317 |
| B | HOH323 |
| B | HOH503 |
| D | PRO-1 |
| D | PHE25 |
| D | VAL90 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 207 |
| Chain | Residue |
| B | PRO-1 |
| B | GLU23 |
| B | HOH322 |
| B | HOH344 |
| B | HOH485 |
| B | HOH506 |
| D | VAL132 |
| D | LYS133 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 201 |
| Chain | Residue |
| C | ARG55 |
| C | ALA101 |
| C | ASN102 |
| C | VAL113 |
| C | HIS126 |
| C | HOH379 |
| C | HOH433 |
| C | HOH542 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 202 |
| Chain | Residue |
| C | HIS0 |
| C | THR2 |
| C | ASN27 |
| C | HOH492 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 203 |
| Chain | Residue |
| C | HIS0 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 204 |
| Chain | Residue |
| C | PRO-1 |
| C | HIS0 |
| C | GLU23 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 201 |
| Chain | Residue |
| D | PHE88 |
| D | PHE124 |
| D | LYS125 |
| D | GOL204 |
| D | HOH386 |
| D | HOH480 |
| D | HOH500 |
| A | ILE67 |
| A | THR68 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 202 |
| Chain | Residue |
| D | ARG55 |
| D | PHE60 |
| D | ALA101 |
| D | ASN102 |
| D | HIS126 |
| D | HOH351 |
| D | HOH507 |
| D | HOH525 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 203 |
| Chain | Residue |
| B | PRO95 |
| D | HIS0 |
| D | THR2 |
| D | ASN27 |
| D | HOH320 |
| D | HOH485 |
| D | HOH497 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 204 |
| Chain | Residue |
| D | ASP85 |
| D | PHE88 |
| D | GOL201 |
| D | HOH324 |
| D | HOH399 |
| D | HOH422 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 205 |
| Chain | Residue |
| B | PRO95 |
| B | HOH361 |
| B | HOH527 |
| D | HIS0 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 206 |
| Chain | Residue |
| B | VAL132 |
| B | HOH506 |
| D | PRO-1 |
| D | HIS0 |
| D | GLU23 |
| D | HOH482 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 201 |
| Chain | Residue |
| E | HIS0 |
| E | THR2 |
| E | ASN27 |
| E | HOH317 |
| E | HOH501 |
| F | PRO95 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL E 202 |
| Chain | Residue |
| E | HIS0 |
| E | MET1 |
| F | PRO95 |
| F | HOH334 |
| site_id | CC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TLA E 203 |
| Chain | Residue |
| E | PRO-1 |
| E | PHE25 |
| E | ILE28 |
| E | VAL90 |
| E | HOH311 |
| E | HOH325 |
| E | HOH330 |
| E | HOH479 |
| F | PRO-1 |
| F | PHE25 |
| F | VAL90 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 204 |
| Chain | Residue |
| E | PRO-1 |
| E | HIS0 |
| E | GLU23 |
| E | HOH483 |
| E | HOH500 |
| F | VAL132 |
| F | LYS133 |
| site_id | CC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL F 201 |
| Chain | Residue |
| F | ARG55 |
| F | PHE60 |
| F | ALA101 |
| F | ASN102 |
| F | HIS126 |
| F | HOH366 |
| F | HOH492 |
| F | HOH495 |
| F | HOH546 |
| site_id | DC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 202 |
| Chain | Residue |
| E | PRO95 |
| E | HOH396 |
| F | HIS0 |
| F | THR2 |
| F | ASN27 |
| F | HOH328 |
| F | HOH477 |
| F | HOH534 |
| site_id | DC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL F 203 |
| Chain | Residue |
| E | HOH368 |
| F | HIS0 |
| F | MET1 |
| site_id | DC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 204 |
| Chain | Residue |
| E | VAL132 |
| E | LYS133 |
| E | HOH483 |
| F | PRO-1 |
| F | HIS0 |
| F | GLU23 |
| F | HOH329 |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. FknSiFHRVIpdFVcQGG |
| Chain | Residue | Details |
| A | PHE48-GLY65 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 936 |
| 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 | 6 |
| Details | Repeat: {"description":"20","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Repeat: {"description":"21","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Repeat: {"description":"22","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
