2X2C
acetyl-CypA:cyclosporine complex
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
C [auth K] | SCOP2B Superfamily | Cyclophilin-like | 8043341 | 3000168 | SCOP2B (2022-06-29) |
E [auth M] | SCOP2B Superfamily | Cyclophilin-like | 8043341 | 3000168 | SCOP2B (2022-06-29) |
F [auth O] | SCOP2B Superfamily | Cyclophilin-like | 8043341 | 3000168 | SCOP2B (2022-06-29) |
H [auth Q] | SCOP2B Superfamily | Cyclophilin-like | 8043341 | 3000168 | SCOP2B (2022-06-29) |
J [auth S] | SCOP2B Superfamily | Cyclophilin-like | 8043341 | 3000168 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
C [auth K] | Pro_isomerase | e2x2cK1 | A: beta barrels | X: Cyclophilin-like (From Topology) | H: Cyclophilin-like (From Topology) | T: Cyclophilin-like | F: Pro_isomerase | ECOD (1.6) |
E [auth M] | Pro_isomerase | e2x2cM1 | A: beta barrels | X: Cyclophilin-like (From Topology) | H: Cyclophilin-like (From Topology) | T: Cyclophilin-like | F: Pro_isomerase | ECOD (1.6) |
F [auth O] | Pro_isomerase | e2x2cO1 | A: beta barrels | X: Cyclophilin-like (From Topology) | H: Cyclophilin-like (From Topology) | T: Cyclophilin-like | F: Pro_isomerase | ECOD (1.6) |
H [auth Q] | Pro_isomerase | e2x2cQ1 | A: beta barrels | X: Cyclophilin-like (From Topology) | H: Cyclophilin-like (From Topology) | T: Cyclophilin-like | F: Pro_isomerase | ECOD (1.6) |
J [auth S] | Pro_isomerase | e2x2cS1 | A: beta barrels | X: Cyclophilin-like (From Topology) | H: Cyclophilin-like (From Topology) | T: Cyclophilin-like | F: Pro_isomerase | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
C [auth K] | 2.40.100.10 | Mainly Beta | Beta Barrel | Cyclophilin | Cyclophilin-like | CATH (4.3.0) |
E [auth M] | 2.40.100.10 | Mainly Beta | Beta Barrel | Cyclophilin | Cyclophilin-like | CATH (4.3.0) |
F [auth O] | 2.40.100.10 | Mainly Beta | Beta Barrel | Cyclophilin | Cyclophilin-like | CATH (4.3.0) |
H [auth Q] | 2.40.100.10 | Mainly Beta | Beta Barrel | Cyclophilin | Cyclophilin-like | CATH (4.3.0) |
J [auth S] | 2.40.100.10 | Mainly Beta | Beta Barrel | Cyclophilin | Cyclophilin-like | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
C [auth K], E [auth M], F [auth O], H [auth Q], J [auth S] | PF00160 | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD (Pro_isomerase) | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD | The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organisms studied so far and catalyse peptidyl-prolyl isomerisation during which the peptide bond pr ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Pharos: Disease Associations Pharos Homepage Annotation
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
A [auth B], B [auth F], D [auth L], G [auth P], I [auth R] | ABA | Parent Component: ALA :  AA0253 , AA0409 :  S-(2-aminovinyl)-3-methyl-D-cysteine MOD:00258 , L-2-aminobutanoic acid (Glu) MOD:00819 |
A [auth B], B [auth F], D [auth L], G [auth P], I [auth R] | BMT | Parent Component: THR :  AA0253 , AA0409 |
A [auth B], B [auth F], D [auth L], G [auth P], I [auth R] | DAL | AA0253 , AA0409 , AA0111 , AA0191 :  S-(2-aminovinyl)-3-methyl-D-cysteine MOD:00258 , L-2-aminobutanoic acid (Glu) MOD:00819 , meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 | : 
A [auth B], B [auth F], D [auth L], G [auth P], I [auth R] | MLE | Parent Component: LEU :  AA0253 , AA0409 , AA0111 , AA0191 , AA0337 :  S-(2-aminovinyl)-3-methyl-D-cysteine MOD:00258 , L-2-aminobutanoic acid (Glu) MOD:00819 , meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 , N-methyl-L-leucine MOD:00342 |
A [auth B], B [auth F], D [auth L], G [auth P], I [auth R] | MVA | Parent Component: VAL :  AA0253 , AA0409 , AA0111 , AA0191 , AA0337 |
A [auth B], B [auth F], D [auth L], G [auth P], I [auth R] | SAR | Parent Component: GLY :  AA0253 , AA0409 , AA0111 , AA0191 , AA0337 , AA0063 :  S-(2-aminovinyl)-3-methyl-D-cysteine MOD:00258 , L-2-aminobutanoic acid (Glu) MOD:00819 , meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 , N-methyl-L-leucine MOD:00342 , N-methylglycine MOD:00072 |
C [auth K], E [auth M], F [auth O], H [auth Q], J [auth S] | ALY | Parent Component: LYS :  AA0253 , AA0409 , AA0111 , AA0191 , AA0337 , AA0063 , AA0055 :  S-(2-aminovinyl)-3-methyl-D-cysteine MOD:00258 , L-2-aminobutanoic acid (Glu) MOD:00819 , meso-lanthionine MOD:00120 , D-alanine (Ala) MOD:00198 , D-alanine (Ser) MOD:00858 , D-alanine MOD:00862 , N-methyl-L-leucine MOD:00342 , N-methylglycine MOD:00072 , N6-acetyl-L-lysine MOD:00064 |