2WAS
Structure of the fungal type I FAS PPT domain
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | 4'-phosphopantetheinyl transferase | 8074379 | 3000948 | SCOP2B (2022-06-29) |
E | SCOP2B Superfamily | 4'-phosphopantetheinyl transferase | 8074379 | 3000948 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | 4'-phosphopantetheinyl transferase | 8074379 | 3000948 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | 4'-phosphopantetheinyl transferase | 8074379 | 3000948 | SCOP2B (2022-06-29) |
C | SCOP2 Family | Holo-(acyl carrier protein) synthase ACPS | 8074378 | 4003652 | SCOP2 (2022-06-29) |
C | SCOP2 Superfamily | 4'-phosphopantetheinyl transferase | 8074379 | 3000948 | SCOP2 (2022-06-29) |
F | SCOP2B Superfamily | 4'-phosphopantetheinyl transferase | 8074379 | 3000948 | 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) |
---|---|---|---|---|---|---|---|---|
A | ACPS_1 | e2wasA1 | A: a+b three layers | X: Bacillus chorismate mutase-like | H: 4'-phosphopantetheinyl transferase (From Topology) | T: 4'-phosphopantetheinyl transferase | F: ACPS_1 | ECOD (1.6) |
E | ACPS_1 | e2wasE1 | A: a+b three layers | X: Bacillus chorismate mutase-like | H: 4'-phosphopantetheinyl transferase (From Topology) | T: 4'-phosphopantetheinyl transferase | F: ACPS_1 | ECOD (1.6) |
D | ACPS_1 | e2wasD1 | A: a+b three layers | X: Bacillus chorismate mutase-like | H: 4'-phosphopantetheinyl transferase (From Topology) | T: 4'-phosphopantetheinyl transferase | F: ACPS_1 | ECOD (1.6) |
B | ACPS_1 | e2wasB1 | A: a+b three layers | X: Bacillus chorismate mutase-like | H: 4'-phosphopantetheinyl transferase (From Topology) | T: 4'-phosphopantetheinyl transferase | F: ACPS_1 | ECOD (1.6) |
C | ACPS_1 | e2wasC1 | A: a+b three layers | X: Bacillus chorismate mutase-like | H: 4'-phosphopantetheinyl transferase (From Topology) | T: 4'-phosphopantetheinyl transferase | F: ACPS_1 | ECOD (1.6) |
F | ACPS_1 | e2wasF1 | A: a+b three layers | X: Bacillus chorismate mutase-like | H: 4'-phosphopantetheinyl transferase (From Topology) | T: 4'-phosphopantetheinyl transferase | F: ACPS_1 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.90.470.20 | Alpha Beta | Alpha-Beta Complex | Ribosomal Protein L22 | Chain A | CATH (4.3.0) |
E | 3.90.470.20 | Alpha Beta | Alpha-Beta Complex | Ribosomal Protein L22 | Chain A | CATH (4.3.0) |
D | 3.90.470.20 | Alpha Beta | Alpha-Beta Complex | Ribosomal Protein L22 | Chain A | CATH (4.3.0) |
B | 3.90.470.20 | Alpha Beta | Alpha-Beta Complex | Ribosomal Protein L22 | Chain A | CATH (4.3.0) |
C | 3.90.470.20 | Alpha Beta | Alpha-Beta Complex | Ribosomal Protein L22 | Chain A | CATH (4.3.0) |
F | 3.90.470.20 | Alpha Beta | Alpha-Beta Complex | Ribosomal Protein L22 | Chain A | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF01648 | 4'-phosphopantetheinyl transferase superfamily (ACPS) | 4'-phosphopantetheinyl transferase superfamily | Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of ... | Domain | |
PF01648 | 4'-phosphopantetheinyl transferase superfamily (ACPS) | 4'-phosphopantetheinyl transferase superfamily | Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of Pfam:PF00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of ... | Domain |