Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS2 and DEBS3: the B domain
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
| Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
|---|---|---|---|---|---|---|---|---|
| B | d1pzrb_ | All alpha proteins | HLH-like | Docking domain B of the erythromycin polyketide synthase (DEBS) | Docking domain B of the erythromycin polyketide synthase (DEBS) | Erythronolide synthase | (Saccharopolyspora erythraea ) [TaxId: 1836 ], | SCOPe (2.08) |
| A | d1pzra_ | All alpha proteins | HLH-like | Docking domain B of the erythromycin polyketide synthase (DEBS) | Docking domain B of the erythromycin polyketide synthase (DEBS) | Erythronolide synthase | (Saccharopolyspora erythraea ) [TaxId: 1836 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
| Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
|---|---|---|---|---|---|
| B | SCOP2B Superfamily | PKS docking domain-like | 8055901 | 3002322 | SCOP2B (2022-06-29) |
| A | SCOP2 Family | Docking domain B of the erythromycin polyketide synthase (DEBS) | 8027089 | 4000657 | SCOP2 (2022-06-29) |
| A | SCOP2 Superfamily | Docking domain B of the erythromycin polyketide synthase (DEBS) | 8039468 | 3000897 | SCOP2 (2022-06-29) |
| A | SCOP2B Superfamily | PKS docking domain-like | 8055901 | 3002322 | 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) |
|---|---|---|---|---|---|---|---|---|
| B | e1pzrB1 | A: alpha duplicates or obligate multimers | X: HLH-like | H: HLH, helix-loop-helix DNA-binding domain (From Topology) | T: HLH, helix-loop-helix DNA-binding domain | F: | ECOD (1.6) | |
| A | e1pzrA1 | A: alpha duplicates or obligate multimers | X: HLH-like | H: HLH, helix-loop-helix DNA-binding domain (From Topology) | T: HLH, helix-loop-helix DNA-binding domain | F: | ECOD (1.6) | |
| A | EUF08205 | e1pzrA2 | A: alpha duplicates or obligate multimers | X: Docking domains in modular polyketide synthases | H: Class 1 C-terminal docking domain (From Topology) | T: Class 1 C-terminal docking domain | F: EUF08205 | ECOD (1.6) |
| A | Docking_1 | e1pzrA3 | A: alpha duplicates or obligate multimers | X: Docking domains in modular polyketide synthases | H: Class 1 N-terminal docking domain (From Topology) | T: Class 1 N-terminal docking domain | F: Docking_1 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
| Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
|---|---|---|---|---|---|---|
| B | 6.10.40.10 | Special | Helix non-globular | Histone, subunit A | CATH (4.3.0) | |
| A | 6.10.40.10 | Special | Helix non-globular | Histone, subunit A | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
| Chains | Accession | Name | Description | Comments | Source |
|---|---|---|---|---|---|
| PF08990 | Erythronolide synthase docking domain (Docking) | Erythronolide synthase docking domain | Polyketide synthase (PKS) catalyzes the biosynthesis of polyketides, which are structurally and functionally diverse natural products in microorganisms and plants [1]. Type I modular PKSs are the large, multifunctional enzymes responsible for the pro ... | Domain |














