5FPV

Crystal structure of human JMJD2A in complex with compound KDOAM20A


Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad5fpva_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd5fpvc_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Dd5fpvd_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ed5fpve_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Gd5fpvg_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Hd5fpvh_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd5fpvb_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Fd5fpvf_ All beta proteins Double-stranded beta-helix Clavaminate synthase-like Jumonji domain / Histone demethylase core JMJD2A core HUMAN (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AJmjCe5fpvA1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
CJmjCe5fpvC1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
DJmjCe5fpvD1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
EJmjCe5fpvE1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
GJmjCe5fpvG1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
HJmjCe5fpvH1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
BJmjCe5fpvB1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)
FJmjCe5fpvF1 A: beta sandwichesX: jelly-rollH: Double-stranded beta-helix (From Topology)T: Double-stranded beta-helixF: JmjCECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
C2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
D2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
E2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
G2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
H2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
B2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)
F2.60.120.650 Mainly Beta Sandwich Jelly Rolls CupinCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF02373JmjC domain, hydroxylase (JmjC)JmjC domain, hydroxylaseThe JmjC domain belongs to the Cupin superfamily [3]. JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the ...The JmjC domain belongs to the Cupin superfamily [3]. JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation [5].
Domain
A, B, C, D, E
PF02375jmjN domain (JmjN)jmjN domain- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
LYSINE-SPECIFIC DEMETHYLASE 4A

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D, E
IPR001965Zinc finger, PHD-typeDomain
A, B, C, D, E
IPR002999Tudor domainDomain
A, B, C, D, E
IPR047479Lysine-specific demethylase 4A, first Tudor domainDomain
A, B, C, D, E
IPR003347JmjC domainDomain
A, B, C, D, E
IPR003349JmjN domainDomain
A, B, C, D, E
IPR019787Zinc finger, PHD-fingerDomain
A, B, C, D, E
IPR011011Zinc finger, FYVE/PHD-typeHomologous Superfamily
A, B, C, D, E
IPR047481Lysine-specific demethylase 4A, second Tudor domainDomain
A, B, C, D, E
IPR047482Lysine-specific demethylase 4A, extended PHD fingerDomain
A, B, C, D, E
IPR034732Extended PHD (ePHD) domainDomain
A, B, C, D, E
IPR013083Zinc finger, RING/FYVE/PHD-typeHomologous Superfamily
A, B, C, D, E
IPR040477Lysine-specific demethylase 4-like, Tudor domainDomain