Structure of PDB 6zn4 Chain A

Receptor sequence
>6zn4A (length=406) Species: 264462 (Bdellovibrio bacteriovorus HD100) [Search protein sequence]
TNFDQEALLYHQQGKPGKIEVISSKPCATEKDLSLAYSPGVAAPCKAIAK
DPAKVYDYTAKGNLVAVISNGTAVLGLGNIGPAAGKPVMEGKGILFKQFA
GIDVFDIEVAATDVDVFCNAVRVLEPTFGGINLEDIKAPECFEIEERLKK
EMNIPVFHDDQHGTAIVSGAALLNACSITNRKMETVRIVVNGAGASANSC
AKIFIALGARRENIIMCDSQGVIYKGRTAGMNKYKEYFASETEARTLTEA
LRGADVFVGLSVAGALTPEMLKDMAKDPIIFAMANPEPEITPDKARAARP
DAIIATGRSDYPNQVNNVLGFPSIFRGALDTRSTQINEEMKLAAVHALAK
LAREDVPDKVSATYGGKSFKFGRDYLIPKPFDTRVLLWVAPEVAKAAMKS
GVATRA
3D structure
PDB6zn4 A rotary mechanism for allostery in bacterial hybrid malic enzymes.
ChainA
Resolution1.679 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y52 A88 K107 E149 D150 D174 D175 N300
Catalytic site (residue number reindexed from 1) Y37 A73 K92 E134 D135 D159 D160 N285
Enzyme Commision number 1.1.1.40: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+)).
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 MG A E149 D150 D175 E134 D135 D160
Gene Ontology
Molecular Function
GO:0004470 malic enzyme activity
GO:0004473 malate dehydrogenase (decarboxylating) (NADP+) activity
GO:0008948 oxaloacetate decarboxylase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding

View graph for
Molecular Function
External links
PDB RCSB:6zn4, PDBe:6zn4, PDBj:6zn4
PDBsum6zn4
PubMed33623032
UniProtQ6MM14;
Q6MM15

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