Structure of PDB 3fa4 Chain H

Receptor sequence
>3fa4H (length=282) Species: 5061 (Aspergillus niger) [Search protein sequence]
PMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTA
ASVHGQADLGICTLNDMRANAEMISNISPSTPVIADADTGYGGPIMVART
TEQYSRSGVAAFHIEDQVQKILVDTDTYVTRIRAAVQARQRIGSDIVVIA
RTDSLQTHGYEESVARLRAARDAGADVGFLEGITSREMARQVIQDLAGWP
LLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAAMREAMEKLKR
DGIPGLDKEMTPQMLFRVCGLDESMKVDAQAG
3D structure
PDB3fa4 Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member.
ChainH
Resolution2.18 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y44 T46 G47 A48 D59 D87 D89 H114 E116 R161 E191 N214 T221 S223
Catalytic site (residue number reindexed from 1) Y43 T45 G46 A47 D58 D86 D88 H113 E115 R151 E181 N204 T211 S213
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 MG H D87 D89 D86 D88
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:3fa4, PDBe:3fa4, PDBj:3fa4
PDBsum3fa4
PubMed19133276
UniProtQ2L887

[Back to BioLiP]