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Structure of PDB 1yjx Chain E Binding Site BS01

Receptor Information >1yjx Chain E (length=243) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] AAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYE FDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKA ETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLP SCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLS EEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAME

Ligand information Ligand ID CL InChI InChI=1S/ClH/h1H/p-1 InChIKey VEXZGXHMUGYJMC-UHFFFAOYSA-M SMILES Software SMILES ACDLabs 10.04 CACTVS 3.341 OpenEye OEToolkits 1.5.0 [Cl-] Formula Cl Name CHLORIDE ION ChEMBL DrugBank DB14547 ZINC PDB chain 1yjx Chain F Residue 263 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1yjx Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Resolution 2.8 Å Binding residue (original residue number in PDB) V81 R83 Binding residue (residue number reindexed from 1) V80 R82 Annotation score 1

Enzymatic activity Catalytic site (original residue number in PDB) H11 R62 E89 H186 Catalytic site (residue number reindexed from 1) H10 R61 E88 H185 Enzyme Commision number 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). 5.4.2.4: bisphosphoglycerate mutase.

Gene Ontology Molecular Function GO:0003824 catalytic activity GO:0004082 bisphosphoglycerate mutase activity GO:0004619 phosphoglycerate mutase activity GO:0005515 protein binding GO:0016787 hydrolase activity GO:0016853 isomerase activity GO:0016868 intramolecular phosphotransferase activity GO:0019901 protein kinase binding GO:0046538 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

	Biological Process
GO:0006094	gluconeogenesis
GO:0006096	glycolytic process
GO:0061621	canonical glycolysis

	Cellular Component
GO:0005576	extracellular region
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0016020	membrane
GO:0034774	secretory granule lumen
GO:0070062	extracellular exosome
GO:1904813	ficolin-1-rich granule lumen

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