Structure of PDB 3fa3 Chain M

Receptor sequence
>3fa3M (length=300) Species: 5061 (Aspergillus niger) [Search protein sequence]
PMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTA
ASVHGQADLGICTLNDMRANAEMISNISPSTPVIADADTGYGGPIMVART
TEQYSRSGVAAFHIEDQVQTKRCGHLAGKILVDTDTYVTRIRAAVQARQR
IGSDIVVIARTDSLQTHGYEESVARLRAARDAGADVGFLEGITSREMARQ
VIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAAM
REAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAGGAAFDGGVD
3D structure
PDB3fa3 Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member.
ChainM
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y44 T46 G47 A48 D59 D87 D89 H114 E116 K122 C124 G125 H126 R161 E191 N214 T221 S223
Catalytic site (residue number reindexed from 1) Y43 T45 G46 A47 D58 D86 D88 H113 E115 K121 C123 G124 H125 R160 E190 N213 T220 S222
Enzyme Commision number 4.1.3.30: methylisocitrate 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 MN M D87 K122 D86 K121
BS02 OAF M Y44 T46 G47 A48 C124 G125 R161 E191 N214 P240 Y43 T45 G46 A47 C123 G124 R160 E190 N213 P239
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3fa3, PDBe:3fa3, PDBj:3fa3
PDBsum3fa3
PubMed19133276
UniProtQ2L887

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