2d1p
From PDBWiki
crystal structure of heterohexameric TusBCD proteins, which are crucial for the tRNA modification
| Authors | Numata, T. Fukai, S. Ikeuchi, Y. Suzuki, T. Nureki, O. |
| Citation | Structural Basis for Sulfur Relay to RNA Mediated by Heterohexameric TusBCD Complex PubMed |
| Release date | 2006-02-28 |
| Exp. Method | X-RAY DIFFRACTION |
| Resolution | 2.15 Å |
| Classification | TRANSLATION |
Sequence
Chain A (140 residues): Blast Uniprot EC 2.8.1.-MRGSHHHHHHGSMRFAIVVTGPAYGTQQASSAFQFAQALIADGHELSSVFFYREGVYNANQLTSPASDEFDLVRAWQQLN AQHGVALNICVAAALRRGVVDETEAGRLGLASSNLQQGFTLSGLGALAEASLTCDRVVQFChain B (119 residues): Blast Uniprot
MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA ASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRFChain C (95 residues): Blast Uniprot
MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIILIDYT DFVRLTVKHPSQMAWChain D (140 residues): Blast Uniprot EC 2.8.1.-
MRGSHHHHHHGSMRFAIVVTGPAYGTQQASSAFQFAQALIADGHELSSVFFYREGVYNANQLTSPASDEFDLVRAWQQLN AQHGVALNICVAAALRRGVVDETEAGRLGLASSNLQQGFTLSGLGALAEASLTCDRVVQFChain E (119 residues): Blast Uniprot
MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA ASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRFChain F (95 residues): Blast Uniprot
MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIILIDYT DFVRLTVKHPSQMAWChain G (140 residues): Blast Uniprot EC 2.8.1.-
MRGSHHHHHHGSMRFAIVVTGPAYGTQQASSAFQFAQALIADGHELSSVFFYREGVYNANQLTSPASDEFDLVRAWQQLN AQHGVALNICVAAALRRGVVDETEAGRLGLASSNLQQGFTLSGLGALAEASLTCDRVVQFChain H (119 residues): Blast Uniprot
MKRIAFVFSTAPHGTAAGREGLDALLATSALTDDLAVFFIADGVFQLLPGQKPDAVLARDYIATFKLLGLYDIEQCWVCA ASLRERGLDPQTPFVVEATPLEADALRRELANYDVILRFChain I (95 residues): Blast Uniprot
MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIILIDYT DFVRLTVKHPSQMAW
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| Databases | Visualization tools | Analysis tools | Quarternary structure |
|---|---|---|---|
Categories: D1 | PDB entry | X-RAY DIFFRACTION | TRANSLATION | ESCHERICHIA COLI | 2006 | EC 2.8.1

