Structure of PDB 2alm Chain A Binding Site BS02

Receptor Information
>2alm Chain A (length=412) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSHMKLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFD
VHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQEAVNHANLDVEALN
RDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNV
AMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITP
FAIAGFQALTALSTTEDPTRASIPFDKDRNGFVMGEGSGMLVLESLEHAE
KRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQV
AYVNAAGTSTPANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAVEA
IVTIEAMRHNFVPMTAGTSEVSDYIEANVVYAQGLEKEIPYAISNTFGFG
GHNAVLAFKRWE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2alm Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2alm Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		A218 R226 N227 G228 S306
Binding residue
(residue number reindexed from 1)		A221 R229 N230 G231 S309
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) C164 A303 E314 K332 H337 F394 F396
Catalytic site (residue number reindexed from 1) C167 A306 E317 K335 H340 F397 F399
Enzyme Commision number 2.3.1.179: beta-ketoacyl-[acyl-carrier-protein] synthase II.
Gene Ontology
Molecular Function
GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2alm, PDBe:2alm, PDBj:2alm
PDBsum2alm
PubMed16618705
UniProtQ9FBC2

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