Structure of PDB 3nvl Chain A

Receptor sequence
>3nvlA (length=549) Species: 185431 (Trypanosoma brucei brucei TREU927) [Search protein sequence]
LTLAAHKTLPRRKLVLVVLDGVGIGPRDEYDAVHVAKTPLMDALFNDPKH
FRSICAHGTAVGLPTDADMGNSEVGHNALGAGRVVLQGASLVDDALESGE
IFTSEGYRYLHGAFSQPGRTLHLIGLLSDGGVHSRDNQVYQILKHAGANG
AKRIRVHALYDGRDVPDKTSFKFTDELEEVLAKLREGGCDARIASGGGRM
FVTMDRYEADWSIVERGWRAQVLGEGRAFKSAREALTKFREEDANISDQY
YPPFVIAGDDGRPIGTIEDGDAVLCFNFRGDRVIEMSRAFEEEEFDKFNR
VRLPKVRYAGMMRYDGDLGIPNNFLVPPPKLTRTSEEYLIGSGCNIFALS
ETQKFGHVTYFWNGNRSGKLSEERETFCEIPSDRVQFNQKPLMKSKEITD
AAVDAIKSGKYDMIRINYPNGDMVGHTGDLKATITSLEAVDQSLQRLKEA
VDSVNGVFLITADHGNSDDMVQRDKKGKPVRDAEGNLMPLTSHTLAPVPV
FIGGAGLDPRVQMRTDLPRAGLANVTATFINLMGFEAPSDYEPSLIEVA
3D structure
PDB3nvl Crystal structure of phosphoglycerate mutase from Trypanosoma brucei.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CO A D22 S74 D424 D465 H466 D20 S72 D422 D463 H464
BS02 CO A D319 D424 H428 H495 D317 D422 H426 H493
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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