Structure of PDB 1ejj Chain A Binding Site BS02

Receptor Information
>1ejj Chain A (length=508) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KKPVALIILDGFALRDETYGNAVAQANKPNFDRYWNEYPHTTLKACGEAV
GLPEGQMGNSEVGHLNIGAGRIVYQSLTRINIAIREGEFDRNETFLAAMN
HVKQHGTSLHLFGLLSDGGVHSHIHHLYALLRLAAKEGVKRVYIHGFLDG
RDVGPQTAPQYIKELQEKIKEYGVGEIATLSGRYYSMDRDKRWDRVEKAY
RAMVYGEGPTYRDPLECIEDSYKHGIYDEFVLPSVIVREDGRPVATIQDN
DAIIFYNFRPDRAIQISNTFTNEDFREFDRGPKHPKHLFFVCLTHFSETV
AGYVAFKPTNLDNTIGEVLSQHGLRQLRIAETEKYPHVTFFMSGGREEEF
PGEDRILINSPKVPTYDLKPEMSAYEVTDALLKEIEADKYDAIILNYANP
DMVGHSGKLEPTIKAVEAVDECLGKVVDAILAKGGIAIITADHGNADEVL
TPDGKPQTAHTTNPVPVIVTKKGIKLRDGGILGDLAPTMLDLLGLPQPKE
MTGKSLIV
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 chain1ejj Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ejj Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		D12 S62 D444 H445
Binding residue
(residue number reindexed from 1)		D10 S60 D442 H443
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D12 S62 D154 R261 K336 D403 H407 D444 H445 H462
Catalytic site (residue number reindexed from 1) D10 S60 D152 R259 K334 D401 H405 D442 H443 H460
Enzyme Commision number 5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004619 phosphoglycerate mutase activity
GO:0016853 isomerase activity
GO:0030145 manganese ion binding
GO:0046537 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
GO:0046872 metal ion binding
Biological Process
GO:0006007 glucose catabolic process
GO:0006096 glycolytic process
GO:0030435 sporulation resulting in formation of a cellular spore
GO:0043937 regulation of sporulation
Cellular Component
GO:0005737 cytoplasm
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:1ejj, PDBe:1ejj, PDBj:1ejj
PDBsum1ejj
PubMed10747010
UniProtQ9X519|GPMI_GEOSE 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=gpmI)

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