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5VH6

2.6 Angstrom Resolution Crystal Structure of N-terminal Fragment (residues 1-406) of Elongation Factor G from Bacillus subtilis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0006414biological_processtranslational elongation
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CL A 501
ChainResidue
ATYR186
AARG193
AGLY266
AVAL267
AGLN268
ALEU269

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DWmeqEQeRGITItsA
ChainResidueDetails
AASP51-ALA66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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