Structure of PDB 3rmj Chain A Binding Site BS01

Receptor Information
>3rmj Chain A (length=307) Species: 491 (Neisseria meningitidis serogroup B) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNRVIIFDTTLRDGEQSPGAAMTKEEKIRVARQLEKLGVDIIEAGFAAAS
PGDFEAVNAIAKTITKSTVCSLSRAIERDIRQAGEAVAPAPKKRIHTFIA
TSPIHMEYKLKMKPKQVIEAAVKAVKIAREYTDDVEFSCEDALRSEIDFL
AEICGAVIEAGATTINIPDTVGYSIPYKTEEFFRELIAKTPNGGKVVWSA
HCHNDLGLAVANSLAALKGGARQVECTVNGLGERAGNASVEEIVMALKVR
HDLFGLETGIDTTQIVPSSKLVSTITGYPVQPNKAIVGANAFSETYEIMS
AESVGWA
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain3rmj Chain A Residue 365 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3rmj Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding
Resolution1.95 Å
Binding residue
(original residue number in PDB)		D16 H204 H206 N240
Binding residue
(residue number reindexed from 1)		D13 H201 H203 N237
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q19
Catalytic site (residue number reindexed from 1) Q16
Enzyme Commision number 2.3.3.13: 2-isopropylmalate synthase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0019752 carboxylic acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3rmj, PDBe:3rmj, PDBj:3rmj
PDBsum3rmj
PubMed22352945
UniProtQ9JZG1|LEU1_NEIMB 2-isopropylmalate synthase (Gene Name=leuA)

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