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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 Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA17
AASP81
AASN135

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307
ChainResidueDetails
ASER213
ASER302

220472

PDB entries from 2024-05-29

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