2DKI | pdb_00002dki

Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni, under pressure of xenon gas (12 atm)


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APRK08294e2dkiA4 A: a+b two layersX: FAD-linked reductases, C-terminal domain-likeH: FAD-linked reductases-C (From Topology)T: FAD-linked reductases-CF: PRK08294ECOD (1.6)
APhe_hydrox_dime2dkiA2 A: a+b three layersX: Thioredoxin-likeH: Thioredoxin-like (From Topology)T: Thioredoxin-likeF: Phe_hydrox_dimECOD (1.6)
AFAD_binding_3_3rde2dkiA3 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: FAD/NAD(P)-binding domainF: FAD_binding_3_3rdECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01494FAD binding domain (FAD_binding_3)FAD binding domain- Family
PF07976Phenol hydroxylase, C-terminal dimerisation domain (Phe_hydrox_dim)Phenol hydroxylase, C-terminal dimerisation domainPhenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerisation i ...Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerisation interface. The domain adopts a thioredoxin-like fold [1].
Domain