Structure of PDB 1ejj Chain A Binding Site BS03

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 ID3PG
InChIInChI=1S/C3H7O7P/c4-2(3(5)6)1-10-11(7,8)9/h2,4H,1H2,(H,5,6)(H2,7,8,9)/t2-/m1/s1
InChIKeyOSJPPGNTCRNQQC-UWTATZPHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(C(=O)O)O)OP(=O)(O)O
CACTVS 3.341O[C@H](CO[P](O)(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0C([C@H](C(=O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH](CO[P](O)(O)=O)C(O)=O
ACDLabs 10.04O=P(O)(O)OCC(O)C(=O)O
FormulaC3 H7 O7 P
Name3-PHOSPHOGLYCERIC ACID
ChEMBLCHEMBL1160563
DrugBankDB04510
ZINCZINC000003869934
PDB chain1ejj Chain A Residue 601 [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)		S62 H123 D154 R185 R191 R261 R264 K336 D403 H462
Binding residue
(residue number reindexed from 1)		S60 H121 D152 R183 R189 R259 R262 K334 D401 H460
Annotation score5
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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