- PDB-2c8m: Structure of protein Ta0514, putative lipoate protein ligase from... -
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Basic information
Entry
Database: PDB / ID: 2c8m
Title
Structure of protein Ta0514, putative lipoate protein ligase from T. acidophilum with bound lipoic acid
Components
LIPOATE-PROTEIN LIGASE A
Keywords
LIGASE / LIPOYLATION
Function / homology
Function and homology information
lipoate-protein ligase / lipoate-protein ligase activity / lipoic acid binding / protein lipoylation / protein-containing complex / ATP binding / metal ion binding / cytoplasm Similarity search - Function
Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) catalytic domain profile. / Biotin/lipoate A/B protein ligase family / Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain / Bira Bifunctional Protein; Domain 2 / BirA Bifunctional Protein; domain 2 / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology
Resolution: 1.89→53.3 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.936 / SU B: 7.152 / SU ML: 0.105 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.137 / ESU R Free: 0.131 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THIS ENTRY CONTAINS ATOMS WITH ZERO OCCUPANCY FOR WHICH B-FACTORS HAVE BEEN REFINED.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.239
5132
5 %
RANDOM
Rwork
0.207
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obs
0.208
97539
99.2 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK