Structure of PDB 6zng Chain F

Receptor sequence
>6zngF (length=753) Species: 264462 (Bdellovibrio bacteriovorus HD100) [Search protein sequence]
TTNFDQEALLYHQQGKPGKIEVISSKPCATEKDLSLAYSPGVAAPCKAIA
KDPAKVYDYTAKGNLVAVISNGTAVLGLGNIGPAAGKPVMEGKGILFKQF
AGIDVFDIEVAATDVDVFCNAVRVLEPTFGGINLEDIKAPECFEIEERLK
KEMNIPVFHDDQHGTAIVSGAALLNACSITNRKMETVRIVVNGAGASANS
CAKIFIALGARRENIIMCDSQGVIYKGRTAGMNKYKEYFASETEARTLTE
ALRGADVFVGLSVAGALTPEMLKDMAKDPIIFAMANPEPEITPDKARAAR
PDAIIATGRSDYPNQVNNVLGFPSIFRGALDTRSTQINEEMKLAAVHALA
KLAREGGKSFKFGRDYLIPKPFDTRVLLWVAPEVAKAAMKSGVATRAIED
WDQYRESLEALQGPSKVFIRSAINRVHQNSAANGGELPRIVFPEGTSTKV
LKALATLVEEKICQPILLGYPERVKEKIKALDIPLLNDVSIVHPSSHPKY
FSFVEKLYSLRQRKGINLGEAERLMADPNYFAAMMVNQGEADGMVSGSSI
NYADAVRPILQTIGVYKEGIPAGLNFVLLEDKFLVLADTTVNLNPTAEQC
AQIALQAAKIVEYFGIEPRVAMLSYSNFSGAEGTPRKMKKAAEIARSLRP
DLMIEGDMQADTAVNPEIMERLFPFSGLKGGANVLVFPNLESSNIAYKLI
QQIGKAEVIGPFLTGVRRSANVLQRTTTVDGIVNSVVFTALEAQYIKEVL
KSR
3D structure
PDB6zng A rotary mechanism for allostery in bacterial hybrid malic enzymes.
ChainF
Resolution2.72 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) Y38 A74 K93 E135 D136 D160 D161 N286
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 F Y649 Q683 Y625 Q659
BS02 ACO F R535 K538 Y576 A577 R581 L584 P595 T614 V615 N616 L617 L714 N718 Q748 R511 K514 Y552 A553 R557 L560 P571 T590 V591 N592 L593 L690 N694 Q724
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6zng, PDBe:6zng, PDBj:6zng
PDBsum6zng
PubMed33623032
UniProtQ6MM14;
Q6MM15

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