Structure of PDB 6nds Chain A

Receptor sequence
>6ndsA (length=305) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
MTAFSDLLVVQEVSPRDGLQIEPTWVPTDKKIDLINQLSTMGFSRIEAGS
FVSPKAIPNLRDGEEVFTGITRHKDIIYVGLIPNLKGALRAVEANANELN
LVLSASQTHNLANMRMTKAQSFAGFTEIVEQLQGKTQFNGTVATTFGCPF
EGKISEREVFSLVEHYLKLGIHNITLADTTGMANPVQVKRIVSHVLSLIS
PEQLTLHFHNTRGLGLTNVLAAYEVGARRFDAALGGLGGCPFAPGASGNI
CTEDLVNMCEEIGIPTTIDLDALIQLSRTLPALLGHDTPSQLAKAGRNTD
LHPIP
3D structure
PDB6nds Structure of an HMG-CoA lyase from Acenitobacter baumannii in complex with coenzyme A and 3-methylmalate
ChainA
Resolution1.65 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.3.4: hydroxymethylglutaryl-CoA lyase.
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 COA A V52 S53 I57 N84 G87 R90 N113 M114 R115 V52 S53 I57 N84 G87 R90 N113 M114 R115
BS02 ZN A D17 H207 H209 D17 H207 H209
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004419 hydroxymethylglutaryl-CoA lyase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006552 L-leucine catabolic process
GO:0046951 ketone body biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6nds, PDBe:6nds, PDBj:6nds
PDBsum6nds
PubMed
UniProtA0A0D5YK08

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