Structure of PDB 3rmj Chain A

Receptor sequence
>3rmjA (length=307) Species: 491 (Neisseria meningitidis serogroup B) [Search protein sequence]
TNRVIIFDTTLRDGEQSPGAAMTKEEKIRVARQLEKLGVDIIEAGFAAAS
PGDFEAVNAIAKTITKSTVCSLSRAIERDIRQAGEAVAPAPKKRIHTFIA
TSPIHMEYKLKMKPKQVIEAAVKAVKIAREYTDDVEFSCEDALRSEIDFL
AEICGAVIEAGATTINIPDTVGYSIPYKTEEFFRELIAKTPNGGKVVWSA
HCHNDLGLAVANSLAALKGGARQVECTVNGLGERAGNASVEEIVMALKVR
HDLFGLETGIDTTQIVPSSKLVSTITGYPVQPNKAIVGANAFSETYEIMS
AESVGWA
3D structure
PDB3rmj Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 A D16 H204 H206 N240 D13 H201 H203 N237
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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