Structure of PDB 1nvm Chain E Binding Site BS02

Receptor Information
>1nvm Chain E (length=338) Species: 79676 (Pseudomonas sp. CF600) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TFNPSKKLYISDVTLRDGSHAIRHQYTLDDVRAIARALDKAKVDSIEVAH
GDGLQGSSFNYGFGRHTDLEYIEAVAGEISHAQIATLLLPGIGSVHDLKN
AYQAGARVVRVATHCTEADVSKQHIEYARNLGMDTVGFLMMSHMIPAEKL
AEQGKLMESYGATCIYMADSGGAMSMNDIRDRMRAFKAVLKPETQVGMHA
HHNLSLGVANSIVAVEEGCDRVDASLAGMGAGAGNAPLEVFIAVAERLGW
NHGTDLYTLMDAADDIVRPLQDRPVRVDRETLGLGYAGVYSSFLRHAEIA
AAKYNLKTLDILVELGHRRMVGGQEDMIVDVALDLLAA
Ligand information
Ligand IDOXL
InChIInChI=1S/C2H2O4/c3-1(4)2(5)6/h(H,3,4)(H,5,6)/p-2
InChIKeyMUBZPKHOEPUJKR-UHFFFAOYSA-L
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341		[O-]C(=O)C([O-])=O
OpenEye OEToolkits 1.5.0C(=O)(C(=O)[O-])[O-]
FormulaC2 O4
NameOXALATE ION
ChEMBL
DrugBank
ZINC
PDB chain1nvm Chain E Residue 3510 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1nvm Crystal structure of a bifunctional aldolase-dehydrogenase: Sequestering a reactive and volatile intermediate
Resolution1.7 Å
Binding residue
(original residue number in PDB)		R17 F139 M141 S171 Y291
Binding residue
(residue number reindexed from 1)		R16 F138 M140 S170 Y290
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) D18 H21 H200 H202 Y291
Catalytic site (residue number reindexed from 1) D17 H20 H199 H201 Y290
Enzyme Commision number 4.1.3.39: 4-hydroxy-2-oxovalerate aldolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003852 2-isopropylmalate synthase activity
GO:0005515 protein binding
GO:0008701 4-hydroxy-2-oxovalerate aldolase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
GO:0009098 L-leucine biosynthetic process
GO:0019336 phenol-containing compound catabolic process
GO:0043640 benzoate catabolic process via hydroxylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1nvm, PDBe:1nvm, PDBj:1nvm
PDBsum1nvm
PubMed12764229
UniProtP51016|HOA_PSEUF 4-hydroxy-2-oxovalerate aldolase (Gene Name=dmpG)

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