Structure of PDB 3fa3 Chain O Binding Site BS01

Receptor Information

>3fa3 Chain O (length=301) Species: 5061 (Aspergillus niger) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTA
ASVHGQADLGICTLNDMRANAEMISNISPSTPVIADADTGYGGPIMVART
TEQYSRSGVAAFHIEDQVQTKRCGHLAGKILVDTDTYVTRIRAAVQARQR
IGSDIVVIARTDSLQTHGYEESVARLRAARDAGADVGFLEGITSREMARQ
VIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAAM
REAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAGGAAFDGGVD
L

Ligand information

Ligand ID

InChI

InChI=1S/Mn/q+2

InChIKey

WAEMQWOKJMHJLA-UHFFFAOYSA-N

SMILES

Software	SMILES
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Mn+2]
CACTVS 3.341	[Mn++]

Formula

Name

MANGANESE (II) ION

PDB chain

3fa3 Chain O Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	3fa3 Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member.
Resolution	2.6 Å
Binding residue (original residue number in PDB)	G47 D87
Binding residue (residue number reindexed from 1)	G46 D86
Annotation score	1

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.

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
PDBsum	3fa3
PubMed	19133276
UniProt	Q2L887

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