1EFG

THE CRYSTAL STRUCTURE OF ELONGATION FACTOR G COMPLEXED WITH GDP, AT 2.7 ANGSTROMS RESOLUTION


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AGTP_EFTU_D2e1efgA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: Alanine racemase-CF: GTP_EFTU_D2ECOD (1.6)
AEFG_IVe1efgA3 A: a+b two layersX: Ribosomal protein S5 domain 2-like (From Topology)H: Ribosomal protein S5 domain 2-like (From Topology)T: Ribosomal protein S5 domain 2-likeF: EFG_IVECOD (1.6)
AEFG_Ce1efgA2 A: a+b two layersX: Alpha-beta plaitsH: EF-G C-terminal domain-like (From Topology)T: EF-G C-terminal domain-likeF: EFG_CECOD (1.6)
AMnmE_helical_2nde1efgA4 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: MnmE_helical_2ndECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00679Elongation factor G C-terminus (EFG_C)Elongation factor G C-terminusThis domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.Domain
PF00009Elongation factor Tu GTP binding domain (GTP_EFTU)Elongation factor Tu GTP binding domainThis domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.Domain
PF03144Elongation factor Tu domain 2 (GTP_EFTU_D2)Elongation factor Tu domain 2Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.
Domain
PF03764Elongation factor G, domain IV (EFG_IV)Elongation factor G, domain IVThis domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
ELONGATION FACTOR G
ELONGATION FACTOR G---
ELONGATION FACTOR G---