Structure of PDB 5kgm Chain A Binding Site BS01

Receptor Information
>5kgm Chain A (length=519) Species: 6239 (Caenorhabditis elegans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQI
EAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNE
SLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELY
LHFYGDGRDTSPNSGVGFLEQTLEFLETTGYGKLATVVGRYYAMDRDNRW
ERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEKG
RVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMTQ
YKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFNGG
LEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFIMC
NFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADHGN
AEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTVLA
IMGLPQPAEMTGVSIVQKI
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 chain5kgm Chain A Residue 603 [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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PDB5kgm Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.
Resolution2.95 Å
Binding residue
(original residue number in PDB)		D426 H430 H485
Binding residue
(residue number reindexed from 1)		D406 H410 H465
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D37 S86 D178 R284 K359 D426 H430 D467 H468 H485
Catalytic site (residue number reindexed from 1) D18 S67 D159 R264 K339 D406 H410 D447 H448 H465
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:0005975 carbohydrate metabolic process
GO:0006007 glucose catabolic process
GO:0006096 glycolytic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5kgm, PDBe:5kgm, PDBj:5kgm
PDBsum5kgm
PubMed28368002
UniProtG5EFZ1|GPMI_CAEEL 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=ipgm-1)

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