4lrt/1/1:A/1:C |
| >4lrt-a1-m1-cA (length=334) [Search sequence] |
APRVRITDSTLRDGSHAMAHQFTEEQVRATVHALDAAGVEVIEVSHGDGLGGSSFNYGFS
AVDEIDLVAAAVDEAVNAKIAVLLLPGVGTVRDLKRAHDAGASVARIATHCTEADVSCQH
FAAARELGMETVGFLMLAHRIGPEELARQARIMVDAGAQCVYVVDSAGALVLSDVQARVQ
ALVREIGHEAQVGFHGHQNLSLGVANSVLAYQNGARQIDGALCALGAGAGNSPTEILAAT
FERLNIETGVNVQAALAAAEEVVRPYLPRLPWADRAAIVQGYAGVYSSFLLHAERAAERY
GVPAHEILQRVGEAGYVGGQEDMIIDIAVQLAEE |
| >4lrt-a1-m1-cC (length=335) [Search sequence] |
PRVRITDSTLRDGSHAMAHQFTEEQVRATVHALDAAGVEVIEVSHGDGLGGSSFNYGFSA
VDEIDLVAAAVDEAVNAKIAVLLLPGVGTVRDLKRAHDAGASVARIATHCTEADVSCQHF
AAARELGMETVGFLMLAHRIGPEELARQARIMVDAGAQCVYVVDSAGALVLSDVQARVQA
LVREIGHEAQVGFHGHQNLSLGVANSVLAYQNGARQIDGALCALGAGAGNSPTEILAATF
ERLNIETGVNVQAALAAAEEVVRPYLPRLPWADRAAIVQGYAGVYSSFLLHAERAAERYG
VPAHEILQRVGEAGYVGGQEDMIIDIAVQLAEERH |
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| PDB ID |
4lrt (database links:
RCSB PDB
PDBe
PDBj
PDBsum) |
| Title |
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site |
| Assembly ID |
1 |
| Resolution |
1.5Å |
| Method of structure determination |
X-RAY DIFFRACTION |
| Number of inter-chain contacts |
93 |
| Sequence identity between the two chains |
0.997 |
| PubMed citation |
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Chain 1 |
Chain 2 |
| Model ID |
1 |
1 |
| Chain ID |
A |
C |
| UniProt accession |
D1A3K8 |
D1A3K8 |
| Species |
471852 (Thermomonospora curvata DSM 43183) |
471852 (Thermomonospora curvata DSM 43183) |
| Function annotation |
BioLiP:4lrtA |
BioLiP:4lrtC |
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Switch viewer: [NGL] [JSmol]
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Dimer structure:
Chain 1 in red;
Chain 2 in blue.
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Full biological assembly
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