Structure of PDB 7kzd Chain E

Receptor sequence
>7kzdE (length=437) Species: 1396 (Bacillus cereus) [Search protein sequence]
TTISGHSKDNLALLKCLQGETKEKEFEISNVLPNHKMKEKLFRENKLKID
IDIEKDIFNYSRKNIQKIEFMPVNRLISQSEIDGIIGTLKEVLPTGQFTS
GPFSKKLEEVIGDYLNKKYVIATSSGTDALMVSLLSIGIQPGDEVIMPAN
SFAATENAVLAIGAKPVFVDIDHKSYCIDPLKIEEAITQKTKCILPVHLY
GKQCDMKRIREIADVYQLRIIEDACQAIGSSNLGEYGDIIILSFNPYKNF
GVCGKAGAIVTNNENLAIRCNQYSYHGFEVDKKNKKVLDFGFNSKIDNLQ
AAIGLERIKFLSYNNLKRVFLAQRYIRNLKELEDRELIKLPRMTEDNVWH
LFPIRIINGRRDEVKNKLYQLYNIETDIYYPVLSHKHNTKLVKKNYMQDT
LLNTEQVHKEILHLPLHPNMLLEEQNFVLEGLINVNK
3D structure
PDB7kzd Snapshots along the catalytic path of KabA, a PLP-dependent aminotransferase required for kanosamine biosynthesis in Bacillus cereus UW85.
ChainE
Resolution1.9 Å
3D
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
Enzyme Commision number 2.6.1.1: aspartate transaminase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLR E G132 T133 A160 D229 C231 Q232 S249 N251 K254 G126 T127 A154 D223 C225 Q226 S243 N245 K248
BS02 GUA E Y281 K289 Y275 K283
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7kzd, PDBe:7kzd, PDBj:7kzd
PDBsum7kzd
PubMed33984505
UniProtC0JRF5

[Back to BioLiP]