Structure of PDB 4hnn Chain D

Receptor sequence
>4hnnD (length=308) Species: 29760 (Vitis vinifera) [Search protein sequence]
TSVDDIKSLRLITAIKTPYLPDGRFDLEAYDALVNMQIVDGAEGVIVGGT
TGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTREAIHATEQGFA
VGMHAALHINPYYGKTSLEGLVSHFESVLPMGPTVIYNVPSRTGQDIPPG
VIHTVAQSANLAGVKECVGNDRIKQYTDNRIVVWSGNDDQCHDAKWDYGA
TGVISVTSNLIPGLMRQLLFKGKNPSLNAKIMPLVNWLFEEPNPIGLNTA
LAQLGVVRPVFRLPYVPLPLAKRVEFVNIVKEIGRENFVGEKDVKVLDDD
DFILVGRY
3D structure
PDB4hnn Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T69 Y132 Y156 R161 K184 I223
Catalytic site (residue number reindexed from 1) T50 Y113 Y137 R142 K165 I204
Enzyme Commision number 4.3.3.7: 4-hydroxy-tetrahydrodipicolinate synthase.
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 LYS D N105 E109 N86 E90 MOAD: Kd=0.002mM
BS02 LYS D G73 Q74 M76 W78 H81 Y131 G54 Q55 M57 W59 H62 Y112 MOAD: Kd=0.002mM
Gene Ontology
Molecular Function
GO:0008840 4-hydroxy-tetrahydrodipicolinate synthase activity
GO:0016829 lyase activity
Biological Process
GO:0009089 lysine biosynthetic process via diaminopimelate

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Molecular Function
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Biological Process
External links
PDB RCSB:4hnn, PDBe:4hnn, PDBj:4hnn
PDBsum4hnn
PubMed23354837
UniProtD7U7T8

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