Structure of PDB 5kgn Chain B Binding Site BS03

Receptor Information
>5kgn Chain B (length=521) Species: 6239 (Caenorhabditis elegans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQ
IEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTN
ESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPEL
YLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDN
RWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGE
KGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGM
TQYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFN
GGLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFI
MCNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADH
GNAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTV
LAIMGLPQPAEMTGVSIVQKI
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 chain5kgn Chain B Residue 604 [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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PDB5kgn Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		D426 H430 H485
Binding residue
(residue number reindexed from 1)		D408 H412 H467
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) D19 S68 D160 R266 K341 D408 H412 D449 H450 H467
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:5kgn, PDBe:5kgn, PDBj:5kgn
PDBsum5kgn
PubMed28368002
UniProtG5EFZ1|GPMI_CAEEL 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=ipgm-1)

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