Structure of PDB 3nvl Chain B Binding Site BS01

Receptor Information
>3nvl Chain B (length=549) Species: 185431 (Trypanosoma brucei brucei TREU927) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LTLAAHKTLPRRKLVLVVLDGVGIGPRDEYDAVHVAKTPLMDALFNDPKH
FRSICAHGTAVGLPTDADMGNSEVGHNALGAGRVVLQGASLVDDALESGE
IFTSEGYRYLHGAFSQPGRTLHLIGLLSDGGVHSRDNQVYQILKHAGANG
AKRIRVHALYDGRDVPDKTSFKFTDELEEVLAKLREGGCDARIASGGGRM
FVTMDRYEADWSIVERGWRAQVLGEGRAFKSAREALTKFREEDANISDQY
YPPFVIAGDDGRPIGTIEDGDAVLCFNFRGDRVIEMSRAFEEEEFDKFNR
VRLPKVRYAGMMRYDGDLGIPNNFLVPPPKLTRTSEEYLIGSGCNIFALS
ETQKFGHVTYFWNGNRSGKLSEERETFCEIPSDRVQFNQKPLMKSKEITD
AAVDAIKSGKYDMIRINYPNGDMVGHTGDLKATITSLEAVDQSLQRLKEA
VDSVNGVFLITADHGNSDDMVQRDKKGKPVRDAEGNLMPLTSHTLAPVPV
FIGGAGLDPRVQMRTDLPRAGLANVTATFINLMGFEAPSDYEPSLIEVA
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain3nvl Chain B Residue 553 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3nvl Crystal structure of phosphoglycerate mutase from Trypanosoma brucei.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D22 S74 D424 D465 H466
Binding residue
(residue number reindexed from 1)		D20 S72 D422 D463 H464
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D22 S74 D166 R281 K356 D424 H428 D465 H466 H495
Catalytic site (residue number reindexed from 1) D20 S72 D164 R279 K354 D422 H426 D463 H464 H493
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:0042802 identical protein 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:0006094 gluconeogenesis
GO:0006096 glycolytic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0097014 ciliary plasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3nvl, PDBe:3nvl, PDBj:3nvl
PDBsum3nvl
PubMed22458781
UniProtQ38AH1|PGAMI_TRYB2 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=PGAM)

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