Structure of PDB 5vkt Chain A

Receptor sequence
>5vktA (length=353) Species: 4558 (Sorghum bicolor) [Search protein sequence]
KTAHGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNE
WGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVDSCRTCESCS
TGHENYCPDLVLTSNGVDHHHHGATTKGGFSDVLVVSQDFVVRVPESLPL
DGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGM
TVTVISSSPGKRDEALGRLGADAFLVSHDAAQMKAAAATLDGIIDTVSAG
HQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVAD
CQAMLDFAGEHGVTADIEVVQMDYVNTAIERLEKNDVRYRFVIDVAGSKM
EET
3D structure
PDB5vkt The Enzyme Activity and Substrate Specificity of Two Major Cinnamyl Alcohol Dehydrogenases in Sorghum (Sorghum bicolor), SbCAD2 and SbCAD4.
ChainA
Resolution1.827 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C47 H48 T49 H52 H69 E70 C100 C103 C106 C114 V118 C165 T169 R347
Catalytic site (residue number reindexed from 1) C40 H41 T42 H45 H62 E63 C93 C96 C99 C107 V111 C158 T162 R340
Enzyme Commision number 1.1.1.195: cinnamyl-alcohol dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0045551 cinnamyl-alcohol dehydrogenase activity
GO:0046872 metal ion binding
Biological Process
GO:0009809 lignin biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5vkt, PDBe:5vkt, PDBj:5vkt
PDBsum5vkt
PubMed28606901
UniProtC5XC49

[Back to BioLiP]