Structure of PDB 6zng Chain D

Receptor sequence
>6zngD (length=750) Species: 264462 (Bdellovibrio bacteriovorus HD100) [Search protein sequence]
TNFDQEALLYHQQGKPGKIEVISSKPCATEKDLSLAYSPGVAAPCKAIAK
DPAKVYDYTAKGNLVAVISNGTAVLGLGNIGPAAGKPVMEGKGILFKQFA
GIDVFDIEVAATDVDVFCNAVRVLEPTFGGINLEDIKAPECFEIEERLKK
EMNIPVFHDDQHGTAIVSGAALLNACSITNRKMETVRIVVNGAGASANSC
AKIFIALGARRENIIMCDSQGVIYKGRTAGMNKYKEYFASETEARTLTEA
LRGADVFVGLSVAGALTPEMLKDMAKDPIIFAMANPEPEITPDKARAARP
DAIIATGRSDYPNQVNNVLGFPSIFRGALDTRSTQINEEMKLAAVHALAK
LAREDSFKFGRDYLIPKPFDTRVLLWVAPEVAKAAMKSGVATRAIEDWDQ
YRESLEALQGPSKVFIRSAINRVHQNSAANGGELPRIVFPEGTSTKVLKA
LATLVEEKICQPILLGYPERVKEKIKALDIPLLNDVSIVHPSSHPKYFSF
VEKLYSLRQRKGINLGEAERLMADPNYFAAMMVNQGEADGMVSGSSINYA
DAVRPILQTIGVYKEGIPAGLNFVLLEDKFLVLADTTVNLNPTAEQCAQI
ALQAAKIVEYFGIEPRVAMLSYSNFSGAEGTPRKMKKAAEIARSLRPDLM
IEGDMQADTAVNPEIMERLFPFSGLKGGANVLVFPNLESSNIAYKLIQQI
GKAEVIGPFLTGVRRSANVLQRTTTVDGIVNSVVFTALEAQYIKEVLKSR
3D structure
PDB6zng A rotary mechanism for allostery in bacterial hybrid malic enzymes.
ChainD
Resolution2.72 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) 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 ACO D Y649 Q683 Y622 Q656
BS02 ACO D R535 K538 Y576 A577 R581 L584 P595 T614 V615 N616 L714 N718 K722 R508 K511 Y549 A550 R554 L557 P568 T587 V588 N589 L687 N691 K695
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0016746 acyltransferase activity
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0006108 malate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6zng, PDBe:6zng, PDBj:6zng
PDBsum6zng
PubMed33623032
UniProtQ6MM14;
Q6MM15

[Back to BioLiP]