Structure of PDB 1nvm Chain G

Receptor sequence
>1nvmG (length=339) Species: 79676 (Pseudomonas sp. CF600) [Search protein sequence]
FNPSKKLYISDVTLRDGSHAIRHQYTLDDVRAIARALDKAKVDSIEVAHG
DGLQGSSFNYGFGRHTDLEYIEAVAGEISHAQIATLLLPGIGSVHDLKNA
YQAGARVVRVATHCTEADVSKQHIEYARNLGMDTVGFLMMSHMIPAEKLA
EQGKLMESYGATCIYMADSGGAMSMNDIRDRMRAFKAVLKPETQVGMHAH
HNLSLGVANSIVAVEEGCDRVDASLAGMGAGAGNAPLEVFIAVAERLGWN
HGTDLYTLMDAADDIVRPLQDRPVRVDRETLGLGYAGVYSSFLRHAEIAA
AKYNLKTLDILVELGHRRMVGGQEDMIVDVALDLLAAHK
3D structure
PDB1nvm Crystal structure of a bifunctional aldolase-dehydrogenase: Sequestering a reactive and volatile intermediate
ChainG
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D18 H21 H200 H202 Y291
Catalytic site (residue number reindexed from 1) D16 H19 H198 H200 Y289
Enzyme Commision number 4.1.3.39: 4-hydroxy-2-oxovalerate aldolase.
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 MN G D18 H200 H202 D16 H198 H200
BS02 OXL G R17 F139 M141 S171 H200 Y291 R15 F137 M139 S169 H198 Y289
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

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Molecular Function
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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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