Structure of PDB 7kzd Chain H Binding Site BS01
Receptor Information
>7kzd Chain H (length=438) Species:
1396
(Bacillus cereus) [
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LTTISGHSKDNLALLKCLQGETKEKEFEISNVLPNHKMKEKLFRENKLKI
DIDIEKDIFNYSRKNIQKIEFMPVNRLISQSEIDGIIGTLKEVLPTGQFT
SGPFSKKLEEVIGDYLNKKYVIATSSGTDALMVSLLSIGIQPGDEVIMPA
NSFAATENAVLAIGAKPVFVDIDHKSYCIDPLKIEEAITQKTKCILPVHL
YGKQCDMKRIREIADVYQLRIIEDACQAIGSSNLGEYGDIIILSFNPYKN
FGVCGKAGAIVTNNENLAIRCNQYSYHGFEVDKKNKKVLDFGFNSKIDNL
QAAIGLERIKFLSYNNLKRVFLAQRYIRNLKELEDRELIKLPRMTEDNVW
HLFPIRIINGRRDEVKNKLYQLYNIETDIYYPVLSHKHNTKLVKKNYMQD
TLLNTEQVHKEILHLPLHPNMLLEEQNFVLEGLINVNK
Ligand information
Ligand ID
GUA
InChI
InChI=1S/C5H8O4/c6-4(7)2-1-3-5(8)9/h1-3H2,(H,6,7)(H,8,9)
InChIKey
JFCQEDHGNNZCLN-UHFFFAOYSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
C(CC(=O)O)CC(=O)O
ACDLabs 10.04
O=C(O)CCCC(=O)O
CACTVS 3.341
OC(=O)CCCC(O)=O
Formula
C5 H8 O4
Name
GLUTARIC ACID
ChEMBL
CHEMBL1162495
DrugBank
DB03553
ZINC
ZINC000000388706
PDB chain
7kzd Chain E Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
7kzd
Snapshots along the catalytic path of KabA, a PLP-dependent aminotransferase required for kanosamine biosynthesis in Bacillus cereus UW85.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
F158 N251 K254 H356
Binding residue
(residue number reindexed from 1)
F153 N246 K249 H351
Annotation score
2
Enzymatic activity
Enzyme Commision number
2.6.1.1
: aspartate transaminase.
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
PDBsum
7kzd
PubMed
33984505
UniProt
C0JRF5
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