1PZQ | pdb_00001pzq

Structure of fused docking domains from the erythromycin polyketide synthase (DEBS), a model for the interaction between DEBS 2 and DEBS 3: The A domain


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyDocking domain A of the erythromycin polyketide synthase (DEBS) 8039464 3000887 SCOP2B (2022-06-29)
ASCOP2 FamilyDocking domain A of the erythromycin polyketide synthase (DEBS) 8027085 4000653 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyDocking domain A of the erythromycin polyketide synthase (DEBS) 8039464 3000887 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BUNK_F_TYPEe1pzqB1 A: alpha duplicates or obligate multimersX: Dimerisation interlockH: Docking domain A of the erythromycin polyketide synthase (DEBS) (From Topology)T: Docking domain A of the erythromycin polyketide synthase (DEBS)F: UNK_F_TYPEECOD (1.6)
AUNK_F_TYPEe1pzqA1 A: alpha duplicates or obligate multimersX: Dimerisation interlockH: Docking domain A of the erythromycin polyketide synthase (DEBS) (From Topology)T: Docking domain A of the erythromycin polyketide synthase (DEBS)F: UNK_F_TYPEECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF09277Erythronolide synthase, docking (Erythro-docking)Erythronolide synthase, dockingMembers of this family of docking domains are found in prokaryotic erythronolide synthase. They adopt a structure consisting of a bundle of four alpha-helices, and mediate homodimerisation of the protein, stabilising the resulting complex [1]. Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
Erythronolide synthase -

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B
IPR016035Acyl transferase/acyl hydrolase/lysophospholipaseHomologous Superfamily
A, B
IPR014031Beta-ketoacyl synthase, C-terminalDomain
A, B
IPR015083Polyketide synthase NorB/C/GfsB-E-like, docking domainDomain
A, B
IPR006162Phosphopantetheine attachment sitePTM
A, B
IPR013154Alcohol dehydrogenase-like, N-terminalDomain
A, B
IPR036347Erythronolide synthase, docking domain superfamilyHomologous Superfamily
A, B
IPR049552Polyketide synthase, dehydratase domain, N-terminalDomain
A, B
IPR049900Polyketide synthase, dehydratase domainDomain
A, B
IPR049551Polyketide synthase, dehydratase domain, C-terminalDomain
A, B
IPR016036Malonyl-CoA ACP transacylase, ACP-bindingHomologous Superfamily
A, B
IPR050091Polyketide and Nonribosomal Peptide Biosynthesis EnzymesFamily
A, B
IPR015357Erythronolide synthase EryA2, docking domainDomain
A, B
IPR020841Polyketide synthase, beta-ketoacyl synthase domainDomain
A, B
IPR020807Polyketide/metazoan fatty acid synthase-like, dehydratase domainDomain
A, B
IPR036736ACP-like superfamilyHomologous Superfamily
A, B
IPR014043Acyl transferase domainDomain
A, B
IPR020843Enoylreductase domainDomain
A, B
IPR032821Polyketide synthase, C-terminal extensionDomain
A, B
IPR011032GroES-like superfamilyHomologous Superfamily
A, B
IPR009081Phosphopantetheine binding ACP domainDomain
A, B
IPR020806Polyketide synthase-like, phosphopantetheine-binding domainDomain
A, B
IPR013968Polyketide synthase-like, ketoreductase domainDomain
A, B
IPR016039Thiolase-likeHomologous Superfamily
A, B
IPR001227Acyl transferase domain superfamilyHomologous Superfamily
A, B
IPR036291NAD(P)-binding domain superfamilyHomologous Superfamily
A, B
IPR018201Beta-ketoacyl synthase, active siteActive Site
A, B
IPR014030Beta-ketoacyl synthase-like, N-terminalDomain
A, B
IPR042104Polyketide synthase, dehydratase domain superfamilyHomologous Superfamily
A, B
IPR055123Polyketide synthase extender module SpnB-like, Rossmann fold domainDomain